CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005283
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Flavohemoprotein 
Protein Synonyms/Alias
 Flavohemoglobin; HMP; Hemoglobin-like protein; Nitric oxide dioxygenase; NO oxygenase; NOD 
Gene Name
 hmp 
Gene Synonyms/Alias
 fsrB; hmpA; b2552; JW2536 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
23LLVETGPKLTAHFYDacetylation[1]
40FTHNPELKEIFNMSNacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. 
Sequence Annotation
 DOMAIN 150 255 FAD-binding FR-type.
 NP_BIND 204 207 FAD.
 NP_BIND 268 273 NADP (By similarity).
 NP_BIND 389 392 FAD.
 REGION 1 138 Globin.
 REGION 147 396 Reductase.
 REGION 259 396 NAD or NADP-binding.
 ACT_SITE 95 95 Charge relay system.
 ACT_SITE 135 135 Charge relay system.
 METAL 85 85 Iron (heme proximal ligand).
 BINDING 188 188 FAD.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Detoxification; Direct protein sequencing; FAD; Flavoprotein; Heme; Iron; Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 396 AA 
Protein Sequence
MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA 60
IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW 120
GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV 180
AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG 240
DVVKLVAPAG DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD 300
VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY 360
LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL 396 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0071949; F:FAD binding; IDA:EcoCyc.
 GO:0005504; F:fatty acid binding; IDA:EcoCyc.
 GO:0020037; F:heme binding; IDA:EcoCyc.
 GO:0032843; F:hydroperoxide reductase activity; IDA:EcoCyc.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0008941; F:nitric oxide dioxygenase activity; IDA:EcoCyc.
 GO:0019825; F:oxygen binding; IEA:InterPro.
 GO:0005344; F:oxygen transporter activity; IEA:HAMAP.
 GO:0051409; P:response to nitrosative stress; IMP:EcoCyc.
 GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW. 
Interpro
 IPR017927; Fd_Rdtase_FAD-bd.
 IPR000971; Globin.
 IPR009050; Globin-like.
 IPR012292; Globin_dom.
 IPR023950; Hmp.
 IPR008333; OxRdtase_FAD-bd_dom.
 IPR001433; OxRdtase_FAD/NAD-bd.
 IPR001221; Phe_hydroxylase.
 IPR017938; Riboflavin_synthase-like_b-brl. 
Pfam
 PF00970; FAD_binding_6
 PF00042; Globin
 PF00175; NAD_binding_1 
SMART
  
PROSITE
 PS51384; FAD_FR
 PS01033; GLOBIN 
PRINTS
 PR00410; PHEHYDRXLASE.