ID K2EWU2_9BACT Unreviewed; 770 AA.
AC K2EWU2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=Carbamoyltransferase HypF {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACD_20C00325G0006 {ECO:0000313|EMBL:EKE02845.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE02845.1};
RN [1] {ECO:0000313|EMBL:EKE02845.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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 -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000256|ARBA:ARBA00004711}.
CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00520}.
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:EKE02845.1}.
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DR EMBL; AMFJ01007804; EKE02845.1; -; Genomic_DNA.
DR AlphaFoldDB; K2EWU2; -.
DR UniPathway; UPA00335; -.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
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; 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; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS51163; YRDC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 5..91
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 198..384
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
SQ SEQUENCE 770 AA; 86491 MW; F208C59148CB4607 CRC64;
MVRVRKNIKI VGIIGSKAFI SYVYSLAKKF NLSGWVRCCK EYINIEVEGE NYSVIEFKSA
ICDNAKPMSK VVEFDSNSVP ILNSDRFYVI DNISEFNSAE NVPHDLAICE DCVDKLFDTR
SRKYHYPFVA CDKCGPKYSI VDSLPFTREN SSLREFKYCY ECQDEISRGN FEAGFSNCHA
CGPKIWLKDK GKVYFNQEES FKAAADIINQ EGILLLKSTN CFYLCSSAFS NNAVEKIREI
KVRRDKPLTV MAKNIQEIEK FAYVNDKEKE LLTSKERPVV VLRIKNSEYL ASSIVSGFDR
VGVMLPVNPI HHLLFDRSNF NVLLMSSANK SGSTIEIDNQ TAESKFGEMV DGILFHDLSI
KNGSDDSIVT VANNEKYSFR LARGYAPSNI RIKDTDSCPV VLACGAHQNS TIALTTPDGR
IHVSPYMGDL DTSNVFDLYK KNILLLCRLF NVSPEQAVCD LNTDYFSTKY VKTLKMPYSQ
IQHGYAHLIS CLVDNDIAID TPVIGVIFDG SQYGADQTVW GGEFLVSKNM NYERVAYIPV
FKMIGVKGKE SHIYRLGYSL LQKACIAIDH PVYKNLELTQ EEESMFFSLI NKGGVSSPLT
SSAGKLFDGV AAIVGAARYS YYEEYSALYL ESLADKDCKD IYIIKDYNIK NIDILIQLIA
KDIELNEPVS IILAKFHNTL AKMVAQTSSE ISRKTGIKQV ALSGSVWMNI LLLERTVEEL
KKAGLKPLIH KNISTNDESL SIGQAAYMVH KITRDKSLVD KAETRSLSGK
//
