| Tag | Content |
|---|
| CPLM ID | CPLM-005840 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Carbamoyltransferase HypF |
Protein Synonyms/Alias | Carbamoyl phosphate-converting enzyme HypF; [NiFe]-hydrogenase maturation factor HypF; Hydrogenase maturation protein HypF |
Gene Name | hypF |
Gene Synonyms/Alias | hydA; b2712; JW5433 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 248 | ARKHRPAKPLAVMLP | acetylation | [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 | Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases using carbamoylphosphate as a substrate. It functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide. |
Sequence Annotation | DOMAIN 8 92 Acylphosphatase-like.
DOMAIN 200 376 YrdC-like.
ZN_FING 109 134 C4-type (Potential).
ZN_FING 159 184 C4-type (Potential).
REGION 19 23 Binds to substrate; phosphate group. |
Keyword | 3D-structure; Complete proteome; Metal-binding; Reference proteome; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 750 AA |
Protein Sequence | MAKNTSCGVQ LRIRGKVQGV GFRPFVWQLA QQLNLHGDVC NDGDGVEVRL REDPETFLVQ 60
LYQHCPPLAR IDSVEREPFI WSQLPTEFTI RQSTGGTMNT QIVPDAATCP ACLAEMNTPG 120
ERRYRYPFIN CTHCGPRFTI IRAMPYDRPF TVMAAFPLCP ACDKEYRDPL DRRFHAQPVA 180
CPECGPHLEW VSHGEHAEQE AALQAAIAQL KMGKIVAIKG IGGFHLACDA RNSNAVATLR 240
ARKHRPAKPL AVMLPVADGL PDAARQLLTT PAAPIVLVDK KYVPELCDDI APDLNEVGVM 300
LPANPLQHLL LQELQCPLVM TSGNLSGKPP AISNEQALAD LQGIADGFLI HNRDIVQRMD 360
DSVVRESGEM LRRSRGYVPD ALALPPGFKN VPPVLCLGAD LKNTFCLVRG EQAVLSQHLG 420
DLSDDGIQMQ WREALRLMQN IYDFTPQYVV HDAHPGYVSS QWAREMNLPT QTVLHHHAHA 480
AACLAEHQWP LDGGDVIALT LDGIGMGENG ALWGGECLRV NYRECEHLGG LPAVALPGGD 540
LAAKQPWRNL LAQCLRFVPE WQNYSETASV QQQNWSVLAR AIERGINAPL ASSCGRFFDA 600
VAAALGCAPA TLSYEGEAAC ALEALAASCH GVTHPVTMPR VDNQLDLATF WQQWLNWQAP 660
VNQRAWAFHD ALAQGFAALM REQATMRGIT TLVFSGGVIH NRLLRARLAH YLADFTLLFP 720
QSLPAGDGGL SLGQGVIAAA RWLAGEVQNG 750 |
Gene Ontology | GO:0016743; F:carboxyl- or carbamoyltransferase activity; IDA:EcoCyc. GO:0003725; F:double-stranded RNA binding; IEA:InterPro. GO:0008270; F:zinc ion binding; IDA:EcoCyc. GO:0046944; P:protein carbamoylation; IDA:EcoCyc. GO:0051604; P:protein maturation; IDA:EcoCyc. |
Interpro | |
Pfam | |
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PRINTS | |