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
//