ID F9N5E5_9FIRM Unreviewed; 752 AA.
AC F9N5E5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carbamoyltransferase {ECO:0000256|PIRNR:PIRNR006256};
DE EC=6.2.-.- {ECO:0000256|PIRNR:PIRNR006256};
GN Name=hypF {ECO:0000313|EMBL:EGS35540.1};
GN ORFNames=HMPREF9200_0733 {ECO:0000313|EMBL:EGS35540.1};
OS Veillonella sp. oral taxon 780 str. F0422.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=944564 {ECO:0000313|EMBL:EGS35540.1, ECO:0000313|Proteomes:UP000010295};
RN [1] {ECO:0000313|EMBL:EGS35540.1, ECO:0000313|Proteomes:UP000010295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0422 {ECO:0000313|EMBL:EGS35540.1,
RC ECO:0000313|Proteomes:UP000010295};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUN-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|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:EGS35540.1}.
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DR EMBL; AFUJ01000034; EGS35540.1; -; Genomic_DNA.
DR RefSeq; WP_009353576.1; NZ_AFUJ01000034.1.
DR AlphaFoldDB; F9N5E5; -.
DR eggNOG; COG0068; Bacteria.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000010295; 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; IPR043129; ATPase_NBD.
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; SSF53067; Actin-like ATPase domain; 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 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:UP000010295};
KW Transferase {ECO:0000313|EMBL:EGS35540.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 3..89
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 199..384
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 752 AA; 84175 MW; EA494C8EE5308A13 CRC64;
MKAYTIHVTG IVQGIGFRPF VSKLAHELRL VGTVRNDTSG VEIHIQGVDA DCQLFVERLQ
SELPMHGRID TLRVEPSTVQ SLHSFTIILS QGAKGNAFIG ADMAPCEACL QDIQDPENRR
FHYGFTNCTN CGPRYTIIES TPYDRHKTSM KAFPMCEECQ GEYEDLEGRR YHAEPNACEQ
CGPMFTLQGT DGMVLATGQD AIEQAKEYIQ QGAIVALKGV GGYHLVCDAL QENAVQTLRQ
RKGRPRKPLA VMAGSLETAK QYVYISEKEE ELLLSPARPI VLLRKVTEHN TVAPSVAPGM
ETLGILLPYA PYHYSLVPFN ALWVMTSANR SGDPVLYNDA QALEELQGIA DYILTHNREI
ISPVDDSVVQ VVHDTSIMIR RSRGYVPVSI PVVALEKRST MLAMGADMKA AFAMNRGSHA
ILSPYMGDME HQRVQDLLWS TTKRYEDLFQ LQPTEVIVDA HPNYYTSQCG RIYAEKYQLP
VIEVQHHHAH VASVLAEYNI QEPVLGICFD GTGYGTDGTL WGGEFLYCHQ EHMERMAHLS
YAPLPGGEVA VREPWRQALW YVNQTYPSGG PTVIEEWKKT LPKGWELLEK MMPHMQMIRS
SSGGRLFDTV ASLLGVGHEH LYDAQLAIEL EQLALSERGT ILDMKLDGTV LDTMSLVRSV
IEQLECGESV AKISANFHRT LIYYIGQMAK QCCKERQISH IVLCGGVFQN RILLEGVIRE
LEEYHIHIPN QSPLNDGGIA LGQLWLGNYM NR
//
