ID A0A1T4VD18_9FIRM Unreviewed; 850 AA.
AC A0A1T4VD18;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=acylphosphatase {ECO:0000256|ARBA:ARBA00015991, ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|ARBA:ARBA00012150, ECO:0000256|PROSITE-ProRule:PRU00520};
GN ORFNames=SAMN02745111_00619 {ECO:0000313|EMBL:SKA62461.1};
OS Eubacterium uniforme.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=39495 {ECO:0000313|EMBL:SKA62461.1, ECO:0000313|Proteomes:UP000190814};
RN [1] {ECO:0000313|EMBL:SKA62461.1, ECO:0000313|Proteomes:UP000190814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35992 {ECO:0000313|EMBL:SKA62461.1,
RC ECO:0000313|Proteomes:UP000190814};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUXZ01000004; SKA62461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4VD18; -.
DR STRING; 39495.SAMN02745111_00619; -.
DR OrthoDB; 9808093at2; -.
DR UniPathway; UPA00335; -.
DR Proteomes; UP000190814; Unassembled WGS sequence.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
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; 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:UP000190814};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 7..102
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 248..440
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT ACT_SITE 22
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 850 AA; 96315 MW; CB4B9AC3F954B1FF CRC64;
MKKDKIIKHI KVYGIVQGVG FRPTVSRHAM ESKITGSVCN RGPYVEIYAC GTYEEIEMFL
DLLKHKPPKR SAILKIDVKD VLSDDENYNK YLNDTNEFEI IESKKTAGEI YVSPDIAICD
ECKEELYDKS NRRYLHPFIN CTSCGPRLTI LDNLPYDRHR TSMKIFPMCK ECDSEYHSSE
SRRYDAQPVC CNDCGPAYYM LDMETGKPES DFLEIVKVQK DVSVKDKSLN MITKNTSYKF
KNIGEYSLNT IKRAREIIRD GKIIAVKGIG GFHLCCDGTD DEAVKRLRML KNRPVKPFAV
MMKNMDVVNR ECVIDENQKE ILDGYQKPIL LLNKKNSDET KLANSISIDN ESVGVMLPYA
PVQMLLFDAG DDDEFTDILV MTSGNVSGAP ISHNDEEAYT EIRGFVDAIL TNNRDIRIRT
DDSVMDFFMG EPMMIRRSRG YAPIPYMTSS DFKGEVLAIG GELKNTFCIA KNNIFYPSSY
VGDLADYRTV KALKDSIKRM LDLLECKPEI IVCDKHPKYN STMVAEELSE ELGIKIEYVQ
HHYAHILSNM GCNDFLEENI GVSFDGTGYG DDDTIWGGEI LTCNLDGFTR ETHIKPFFQM
GGDSSSKEGV KIAVSIIFSM FEKEEAYECI EKLNLCEKKD LNLLYMMFDK KMNGVNSTSM
GRLFDAISAV LGIRNKSTFE GESAIYLEYA AEKYLDSRNV KPEYKNKDCM DKYDAINELT
SKIVDGYDTE FLCKNNGFTY EDINETDKLY ADIIKLKLEG KDSGELSFLF HKKISEMVVA
SVKTISRKNN IKTVTLSGGV FQNKLLTYLT KGALEKEGFK VLTHKLLPAN DGGIALGQAL
YGMNKITKNN
//
