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Database: UniProt
Entry: A0A1V2ZWT4_9GAMM
LinkDB: A0A1V2ZWT4_9GAMM
Original site: A0A1V2ZWT4_9GAMM 
ID   A0A1V2ZWT4_9GAMM        Unreviewed;       782 AA.
AC   A0A1V2ZWT4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE            EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN   ORFNames=B1A74_10315 {ECO:0000313|EMBL:OOC09584.1};
OS   Thioalkalivibrio halophilus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=252474 {ECO:0000313|EMBL:OOC09584.1, ECO:0000313|Proteomes:UP000189177};
RN   [1] {ECO:0000313|EMBL:OOC09584.1, ECO:0000313|Proteomes:UP000189177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL17 {ECO:0000313|EMBL:OOC09584.1,
RC   ECO:0000313|Proteomes:UP000189177};
RA   Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA   Sorokin D.Y., Muyzer G.;
RT   "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with
CC       HypE, it catalyzes the synthesis of the CN ligands of the active site
CC       iron of [NiFe]-hydrogenases. HypF functions as a carbamoyl transferase
CC       using carbamoylphosphate as a substrate and transferring the
CC       carboxamido moiety in an ATP-dependent reaction to the thiolate of the
CC       C-terminal cysteine of HypE yielding a protein-S-carboxamide.
CC       {ECO:0000256|PIRNR:PIRNR006256}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + C-terminal L-cysteinyl-[HypE protein] + carbamoyl
CC         phosphate + H2O = AMP + C-terminal S-carboxamide-L-cysteinyl-[HypE
CC         protein] + diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:55636,
CC         Rhea:RHEA-COMP:14247, Rhea:RHEA-COMP:14392, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:76913,
CC         ChEBI:CHEBI:139126, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00001186,
CC         ECO:0000256|PIRNR:PIRNR006256};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC   -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC       {ECO:0000256|ARBA:ARBA00004711, ECO:0000256|PIRNR:PIRNR006256}.
CC   -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC       {ECO:0000256|ARBA:ARBA00008097, ECO:0000256|PIRNR:PIRNR006256}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOC09584.1}.
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DR   EMBL; MUZR01000044; OOC09584.1; -; Genomic_DNA.
DR   RefSeq; WP_077244584.1; NZ_MUZR01000044.1.
DR   AlphaFoldDB; A0A1V2ZWT4; -.
DR   STRING; 252474.B1A74_10315; -.
DR   OrthoDB; 9808093at2; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000189177; Unassembled WGS sequence.
DR   GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.110.120; -; 1.
DR   Gene3D; 3.30.420.360; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.90.870.50; -; 1.
DR   InterPro; IPR001792; Acylphosphatase-like_dom.
DR   InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR   InterPro; IPR017968; Acylphosphatase_CS.
DR   InterPro; IPR004421; Carbamoyltransferase_HypF.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR041440; HypF_C.
DR   InterPro; IPR006070; Sua5-like_dom.
DR   InterPro; IPR011125; Znf_HypF.
DR   NCBIfam; TIGR00143; hypF; 1.
DR   PANTHER; PTHR42959; CARBAMOYLTRANSFERASE; 1.
DR   PANTHER; PTHR42959:SF1; CARBAMOYLTRANSFERASE HYPF; 1.
DR   Pfam; PF00708; Acylphosphatase; 1.
DR   Pfam; PF17788; HypF_C; 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/BLUF domain-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
DR   PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR   PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189177};
KW   Transferase {ECO:0000313|EMBL:OOC09584.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          8..94
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          205..390
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ   SEQUENCE   782 AA;  82852 MW;  21A6D56043B4F1D3 CRC64;
     MNDPARARWR LIVAGRVQGV GFRPFVARQA RRLGLTGAVA NTPEGVVIEI EGPQAALSSF
     RRSLEEDGPP AARVDLITAT TIPPLGDADF YVRTNHAAGG GAPALAPDRA PCPACRAEIR
     DPAARRFRYP FTACADCGPR WSIATDLPWD RAHTTLAAFP LCPACRTEFE DPEDRRFHAE
     AMACPACGPQ LTLRTPDGGA RSTGDDALRA AVDTLREGGI LALKGTGGFQ LLVDATRPEA
     VARLRRRKQR PEKPLAIMLP GRAETDTLAR IDDVERALLE SPEAPIVLVE GRPEAPLAEE
     VAPGLGRRGL MRPSTPLHLL LLDDFGEPVV CTSGNRSGEP LCVEGDEAVA RLGDIADAIL
     DHDRPVARAL DDSVFQVAAG EPQCLRLGRG CMPTRVPLPA GEPAVAPAPV TLALGGQLKA
     APALTLANEV VAGAHVGDLE SDAALRRLDG EARALGSLCG VDIERIACDR HPDYASTRLA
     ETWNLPLTRV QHHHAHAVAA LAEHGVREPA LALVWDGAGL GDDGTLWGGE CLSLDRDGSW
     RRSGHLRPFR LPGGEAAMRE PRRALLGLLH ARYHGDRAAL EASPARALFT AAEWQPLLAC
     LDRGINAPVT SSAGRLFDAV AALSGLRIAA GYEGQAALRV QEAAEAAGPA DNAAQYGDTD
     AITLDTDLAP WQGDWAPLVD ALLAERAARP VDAPARMATR LHRALAGFAV AAARANNRET
     VALTGGCFQN RHLLQQCVDA LRAAGFRPLW PQRIPPGDGG LATGQAVIAR RATSPVRTTD
     GD
//
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