ID G9YIZ1_9FIRM Unreviewed; 764 AA.
AC G9YIZ1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=HMPREF0080_01635 {ECO:0000313|EMBL:EHM39133.1};
OS Anaeroglobus geminatus F0357.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Anaeroglobus.
OX NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM39133.1, ECO:0000313|Proteomes:UP000005481};
RN [1] {ECO:0000313|EMBL:EHM39133.1, ECO:0000313|Proteomes:UP000005481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0357 {ECO:0000313|EMBL:EHM39133.1,
RC ECO:0000313|Proteomes:UP000005481};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- 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|ARBA:ARBA00000744, ECO:0000256|PROSITE-
CC ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711}.
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|ARBA:ARBA00005614}.
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:EHM39133.1}.
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DR EMBL; AGCJ01000072; EHM39133.1; -; Genomic_DNA.
DR RefSeq; WP_006790602.1; NZ_JH417605.1.
DR AlphaFoldDB; G9YIZ1; -.
DR STRING; 861450.HMPREF0080_01635; -.
DR GeneID; 85019799; -.
DR PATRIC; fig|861450.3.peg.1509; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_9; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000005481; 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-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 Reference proteome {ECO:0000313|Proteomes:UP000005481};
KW Transferase {ECO:0000313|EMBL:EHM39133.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 2..88
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 194..384
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 17
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 35
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 764 AA; 83412 MW; 758384AF77DFE555 CRC64;
MTKRICVFGI VQGVGFRPFI SRLAREHGIA GHVCNRGSYV EIVAGGEAAH IEAFQENITK
KAPPRSHIIG LTSIETDDID TAGFSIVESA REEGRVFVSP DIGICDTCAT ELFEPGNRRY
LHPFINCTAC GPRLTILRSM PYDRERTSMG EFPMCPDCAD EYENPASRRY DAQPVCCNEC
GPDVTVMGTD IHGADAVKEA RRAIADGKII AVKGLGGFHL CCDGTREEVV TRLRRLKHRP
VKPFAVMVKD LATAERECVV TNGARSLLTD YERPIVLLRR RPDAEAAITV APGNPYVGIM
LPYAPLQLLL FSYPDDTLVS DVLVMTSANQ SGAPICRTDE EAAAELAEMC DLILTHNRDI
LLRADDSVMA LADDCPYAVR RSRGYAPLPI MAKGDFHGTV VGIGGELKNV FCLGKDNLFY
LSPHIGDMSD VRTVAALRQT IGRMEDLLEI MPGLGACDLH PQYNTTIVAH EQNLPLLPVQ
HHYAHVLSCM AENSCTGPVI GVALDGTGYG TDGTIWGGEI LVADYQAFTR YGSIMPFIHA
GGDAAVRYGW RTALSLLFEL YGRDALRKGV DIYKLCDYRH AAAQFFMLNS GVNCGISTST
GRLFDGVSAL LGFCLSETFE GEAAMNLQFA AEAWVEAHGE TDLPFDVFLR EEPGIFRLAT
TDLVRSLLER KAVGMSADEG AWLFHLALAE LICKGAQEVR CRTGLEEVCL SGGVFQNLLL
LRLCKCRLEE AHFHVYTHHL VPTNDGGIAL GQAVAAMVLK NKGE
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