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Database: UniProt
Entry: Q55638
LinkDB: Q55638
Original site: Q55638 
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   16-APR-2014, entry version 101.
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   KEGG; syz:MYO_122090; -.
DR   PATRIC; 23841762; VBISynSp132158_2428.
DR   eggNOG; COG0068; -.
DR   HOGENOM; HOG000278743; -.
DR   KO; K04656; -.
DR   OMA; FTNCTNC; -.
DR   OrthoDB; EOG6ND0QX; -.
DR   PhylomeDB; Q55638; -.
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_dom.
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   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; SSF54975; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00143; hypF; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
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
//
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