ID A0A1F8QGW4_9CHLR Unreviewed; 806 AA.
AC A0A1F8QGW4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN ORFNames=A2Z16_09525 {ECO:0000313|EMBL:OGO34663.1};
OS Chloroflexi bacterium RBG_16_54_18.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797648 {ECO:0000313|EMBL:OGO34663.1, ECO:0000313|Proteomes:UP000177170};
RN [1] {ECO:0000313|EMBL:OGO34663.1, ECO:0000313|Proteomes:UP000177170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|PROSITE-ProRule:PRU00520};
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711}.
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:OGO34663.1}.
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DR EMBL; MGNP01000015; OGO34663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8QGW4; -.
DR STRING; 1797648.A2Z16_09525; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000177170; 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 Transferase {ECO:0000313|EMBL:OGO34663.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..92
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 210..404
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 806 AA; 89408 MW; 67CAE59893EA3602 CRC64;
MGELSGAIIE IKGIVQGVGF RPFVYSLASQ LMLKGWVRNT SAGVDIQVDG SPEMITSFLE
SLRYNAPPLA RIDALQVENC APQGFSIFEI IHSKPTPGAF QPISPDVCIC PDCLSELLNP
SDRRYLYPFI NCTNCGPRFT IIQDIPYDRP NTTMSGFPMC LECAVEYADP TDRRFHAQPV
ACHVCGPHIW LEFRGEKPVS EKGLDRERSR SDLVSSQRLL LEGKILAIKG LGGFHLACDA
QNAEAVAELR RRKLRVDKPF AVMMPDIETI EQHCQVSESE RTLLESRQRP IVILNRLRSS
TVAEMVAPGQ TTIGVMLPYT PLHYLLVSDL QEEYAINPAQ VLVMTSGNLS EEPIATDNDV
ARKRLASLAD AFLMHNRPIH TRCDDSVARI IDLKLPAENQ NGGNAKQYSY YPIRRSRGYA
PDAIKLPWEM TEILAAGAEL KNTFCLTKQD YAFISHHIGD LENYETLCAF EDGVAHYERL
FRIKPSVIAY DLHPDYLASR YALQRAERDS LPACGVQHHH AHIASCMAEH HLPADQRVIG
VSFDGTGFGE DGCIWGGEFL VCGYDSYTRP YHLRYTPLPG GDKAIREPWR MALSWMSTAG
IPWDESLPPL RYQVQKEANY MQRLDVLQRQ IQSGLNAPPT SSIGRLFDAV AAIIGIKQVV
NYEAQAAIEL EALATEDESG AYSFTIESGR ARLEGTGRSA GVFDPEPVFS AILEDMEKGV
SQALISARFH NGLAQVVREI CNELREETGF DVVALSGGVW QNVKLLRITK KLLNNAGFNV
LIHRQVPAND GGIALGQAVV AANRLV
//