ID A0A0T5NWG6_9RHOB Unreviewed; 781 AA.
AC A0A0T5NWG6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:QEW30067.1};
GN ORFNames=RIdsm_05913 {ECO:0000313|EMBL:QEW30067.1}, XM52_27875
GN {ECO:0000313|EMBL:KRS13275.1};
OS Roseovarius indicus.
OG Plasmid pRIdsm_03 {ECO:0000313|EMBL:QEW30067.1}, and
OG Plasmid pridsm_03 {ECO:0000313|Proteomes:UP000325785}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS13275.1, ECO:0000313|Proteomes:UP000051401};
RN [1] {ECO:0000313|EMBL:KRS13275.1, ECO:0000313|Proteomes:UP000051401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B108 {ECO:0000313|EMBL:KRS13275.1,
RC ECO:0000313|Proteomes:UP000051401};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius indicus B108T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEW30067.1, ECO:0000313|Proteomes:UP000325785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW30067.1,
RC ECO:0000313|Proteomes:UP000325785};
RC PLASMID=pRIdsm_03 {ECO:0000313|EMBL:QEW30067.1}, and pridsm_03
RC {ECO:0000313|Proteomes:UP000325785};
RA Vollmers J., Petersen J.;
RT "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT geographic distances.";
RL Submitted (AUG-2018) 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}.
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DR EMBL; LAXI01000038; KRS13275.1; -; Genomic_DNA.
DR EMBL; CP031601; QEW30067.1; -; Genomic_DNA.
DR RefSeq; WP_037240020.1; NZ_FOMY01000018.1.
DR AlphaFoldDB; A0A0T5NWG6; -.
DR STRING; 540747.SAMN04488031_11826; -.
DR KEGG; rid:RIdsm_05913; -.
DR PATRIC; fig|540747.5.peg.4361; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000051401; Unassembled WGS sequence.
DR Proteomes; UP000325785; Plasmid pridsm_03.
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-UniRule.
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 Plasmid {ECO:0000313|EMBL:QEW30067.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051401};
KW Transferase {ECO:0000313|EMBL:KRS13275.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..87
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 201..385
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 781 AA; 84618 MW; 953FE769472DDE8F CRC64;
MTGARFTVSG QVQGVGFRPT VWRLAHEMGL TGDVKNTGEG VVIQLWGDHV ATFPDRLHSA
LPPLARIERL DVTPLTDPAP CGFEITASQE GEMRGNVTPD AATCADCLEE IRNPFERRYR
YPFANCTNCG PRFSIVQAAP YDRAKTTMAP FDFCPPCEAE YSNPVDRRFH AQPVACGRCG
PNIWIEKLGK GAVNLEAFSM LDDVDATGGM IMNGHIVAIR GLGGVHLACD ATNAAAVAEL
RRRKSRTGKA FALMARDLDV VRAYCEVSKI EADLLSSPQA PIVLLKAKPN GLPSEIAPGL
DRLGVMLPYT PFYHMILRRI GRPVIMTSGN PSGQPQCIDN QETRDRLADI ADFACLHNRD
IANRIDDSVV RVDLGRPRVL RRARGYAPQG LELPAGFSDA LEVLALGAEQ KNTFCLVKDA
RAIMSQHMGD LEDVATNADV TRNLGLYENL FDHAPDIIAV DQHPQYLSTQ RGFQMAGDRP
VIQVQHHHAH IAACLVENNR PLSAEHVLGI ALDGTGLGDD GTIWGGEFLI CDYHGYRRVG
CLKPVALPGG VAAVREPWRN AYAHLMAEMG WGEFAINFPD LEVFSRMRDL PRDTLDAMIK
SGTNSPLASS CGRLFDAAAA IAGIAWDRQN YEGEAAILFE AALDPDALNE PDDLAYPFSI
PLMGGKGMPY IEPLAVWRAM LGDLVLQTPI GTISARFHRG LARAIVEMAV RLTKDTAIDT
VALSGGCFQN ATLFALVHQG LEGAELTVLS HSDYPANDGG ISLGQAVIAL ANTQGEDAKC
A
//