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Database: UniProt
Entry: A0A1K1M2R0_9FIRM
LinkDB: A0A1K1M2R0_9FIRM
Original site: A0A1K1M2R0_9FIRM 
ID   A0A1K1M2R0_9FIRM        Unreviewed;       774 AA.
AC   A0A1K1M2R0;
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=SAMN02910447_00533 {ECO:0000313|EMBL:SFW16214.1};
OS   Ruminococcus sp. YE71.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=244362 {ECO:0000313|EMBL:SFW16214.1, ECO:0000313|Proteomes:UP000182164};
RN   [1] {ECO:0000313|EMBL:SFW16214.1, ECO:0000313|Proteomes:UP000182164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YE71 {ECO:0000313|EMBL:SFW16214.1,
RC   ECO:0000313|Proteomes:UP000182164};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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};
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00520}.
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DR   EMBL; FPIR01000002; SFW16214.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1K1M2R0; -.
DR   STRING; 244362.SAMN02910447_00533; -.
DR   UniPathway; UPA00335; -.
DR   Proteomes; UP000182164; 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182164};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          5..94
FT                   /note="Acylphosphatase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51160"
FT   DOMAIN          200..390
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51163"
SQ   SEQUENCE   774 AA;  84920 MW;  4FD66D6513DB44E6 CRC64;
     MALKTVRMKI FGIVQGVGFR PFMAVSAEKT GVCGTVANKG SYVEAIVQGS GEQIDRYADI
     VRNSPPERSV ILGLDIDPCE DGEFPEFADF RIIESKKEYG DIFVSPDIAT CDKCRTELFD
     KNDRRYLHPF INCTQCGPRL TILDTMPYDR VRTSMGEFPM CSECDSEYHD PATRRYDAQP
     VCCNDCGPRV RILGTDIFDG DAIRLIRREI MAGKVAAVKG IGGFHLCCDA HNAAAVARLR
     ELKRRPMKPF AVMMRDFETT ERECFVAEGQ REYLTGWQKP ILLLERRPDS TLSEQIAPDN
     DTVGVMLPYA PVQMLLFDYP DGLDFTDCLV MTSGNARGAP ICRSDEDALA EIPGFCDYIL
     THDRKIRIRA DDSVCDWLFG KPYMIRRSRG FAPLPVMLHG GEGRQAIGIG GELKNTFCIA
     RNGLLYASPY VGDMADIRTV RALKESVHRM IGLLEAEPEV IVCDTHPMYN TVTVAEELAE
     EMGLPLVKIQ HHFAHILSCM AENRLAPDSR VIGVSFDGTG YGDDGTIWGG ELMICGYGSY
     ERVGSVAPFM QCGGDLSSKE GWRIAVQLIR QGFGEDAQAV CERLGLCDAK TFKIQSAMAD
     KRVNSVLSTS CGRIFDAVSA ILGIRQASTF EGEASTALMT AAERYVKQNG ETKLTLPIEM
     TADTESGSGF ITLGSSALAA EIARRFMDGG DAGQLAFEFH AALSELIRIA CIELREKHGL
     NEVALSGGVF QNRLLVKLTK AALEKAGFTV LLHTLIPPND GGICVGQAAH GVLK
//
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