ID HYPF_SYNY3 Reviewed; 767 AA.
AC Q55638;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 01-MAY-2013, entry version 95.
DE RecName: Full=Carbamoyltransferase HypF;
DE EC=2.1.3.-;
DE AltName: Full=Carbamoyl phosphate-converting enzyme HypF;
DE AltName: Full=[NiFe]-hydrogenase maturation factor HypF;
DE Short=Hydrogenase maturation protein HypF;
GN Name=hypF; OrderedLocusNames=sll0322;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb
RT region from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT entire genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Along with HypE, it catalyzes the synthesis of the CN
CC ligands of the active site iron of [NiFe]-hydrogenases using
CC carbamoylphosphate as a substrate. It functions as a carbamoyl
CC transferase using carbamoylphosphate as a substrate and
CC transferring the carboxamido moiety in an ATP-dependent reaction
CC to the thiolate of the C-terminal cysteine of HypE yielding a
CC protein-S-carboxamide (By similarity).
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain.
CC -!- SIMILARITY: Contains 1 YrdC-like domain.
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DR EMBL; BA000022; BAA10154.1; -; Genomic_DNA.
DR PIR; S76302; S76302.
DR RefSeq; NP_442084.1; NC_000911.1.
DR RefSeq; YP_005652142.1; NC_017277.1.
DR RefSeq; YP_007451961.1; NC_020286.1.
DR ProteinModelPortal; Q55638; -.
DR IntAct; Q55638; 4.
DR STRING; 1148.sll0322; -.
DR EnsemblBacteria; BAA10154; BAA10154; BAA10154.
DR GeneID; 12253355; -.
DR GeneID; 14617631; -.
DR GeneID; 953323; -.
DR KEGG; syn:sll0322; -.
DR KEGG; syy:SYNGTS_2189; -.
DR PATRIC; 23841762; VBISynSp132158_2428.
DR eggNOG; COG0068; -.
DR HOGENOM; HOG000278743; -.
DR KO; K04656; -.
DR OMA; MACFPLC; -.
DR UniPathway; UPA00335; -.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046944; P:protein carbamoylation; IEA:InterPro.
DR Gene3D; 3.90.870.10; -; 1.
DR InterPro; IPR001792; Acylphosphatase-like.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR004421; Carbamoyltransferase_HypF.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR006070; YrdC-like_dom.
DR InterPro; IPR011125; Znf_HypF.
DR PANTHER; PTHR10029:SF4; PTHR10029:SF4; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR Pfam; PF07503; zf-HYPF; 2.
DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1.
DR SUPFAM; SSF54975; Acylphosphatase; 1.
DR SUPFAM; SSF55821; DHBP_synth_RibB-like_a/b_dom; 1.
DR TIGRFAMs; TIGR00143; hypF; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; FALSE_NEG.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Complete proteome; Metal-binding; Reference proteome; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1 767 Carbamoyltransferase HypF.
FT /FTId=PRO_0000071618.
FT DOMAIN 4 90 Acylphosphatase-like.
FT DOMAIN 200 385 YrdC-like.
FT ZN_FING 107 131 C4-type (Potential).
FT ZN_FING 157 182 C4-type (Potential).
SQ SEQUENCE 767 AA; 85358 MW; FA9BA174172AB60D CRC64;
MLKTVAIQVQ GRVQGVGFRP FVYTLAQEMG LNGWVNNSTQ GATVVITADE KAIADFTERL
TKTLPPPGLI EQLAVEQLPL ESFTNFTIRP SSDGPKTASI LPDLSTCSAC LTELFDPSDR
RYLYPFINCT HCGPRYTIIE ALPYDRCRTT MARFRQCTDC EREYKQPGDR RFHAQPNACP
RCGPQLAFWN RQGQVIAEAN EALNFAVDNL KVGNIIAIKG LGGFHLCCDA TDFEAVEKLR
LRKHRPDKPL AVMYGNLGQI VEHYQPNNLE VELLQSAAAP IVLLNKKKQL ILVENIAPGN
PRVGVMLAYT PLHHLLLKKL KKPMVATSGN LAGEQICIDN IDALTRLQNI ADGFLVHDRP
IVCPVDDSVV QIVAGKPLFL RRARGYAPQP ITLPKPTQKK LLAMGGHYKN TVAIAKQNQA
YVSQHLGDLN SAPTYQNFEE AIAHLSQLYD FSPQEIVADL HPDYFSHQYA ENQALPVTFV
QHHYAHILAV MAEHGVMEES VLGIAWDGTG YGMDGTIWGG EFLKITQGTW QRIAHLQPFH
LLGNQQAIKY PHRIALALLW PTFGDDFSAD SLGNWLNFNN GFKNKINSRL NQDLNNKNLR
QLWQRGQAPL TSSMGRLFDG IATLIGLINE VTFEGQAAIA LEAQIMPNLT EEYYPLTLNN
KEKKLAVDWR PLIKAITTED RSKTNLIATK FHNSLVNLII TIAQQQGIEK VALGGGCFQN
CYLLASTITA LKKAGFSPLW PRELPPNDGA ICMGQLLAKI QARQYIC
//
