ID B6G9X9_9ACTN Unreviewed; 1042 AA.
AC B6G9X9;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 03-MAY-2023, entry version 70.
DE RecName: Full=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN Name=hypF {ECO:0000313|EMBL:EEA90834.1};
GN ORFNames=COLSTE_00870 {ECO:0000313|EMBL:EEA90834.1};
OS Collinsella stercoris DSM 13279.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90834.1, ECO:0000313|Proteomes:UP000003560};
RN [1] {ECO:0000313|EMBL:EEA90834.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90834.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEA90834.1, ECO:0000313|Proteomes:UP000003560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90834.1,
RC ECO:0000313|Proteomes:UP000003560};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family.
CC {ECO:0000256|ARBA:ARBA00008097}.
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:EEA90834.1}.
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DR EMBL; ABXJ01000055; EEA90834.1; -; Genomic_DNA.
DR RefSeq; WP_006720532.1; NZ_DS995475.1.
DR AlphaFoldDB; B6G9X9; -.
DR STRING; 445975.COLSTE_00870; -.
DR eggNOG; COG0068; Bacteria.
DR HOGENOM; CLU_009164_0_0_11; -.
DR Proteomes; UP000003560; Unassembled WGS sequence.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 1.10.357.160; -; 1.
DR Gene3D; 3.30.110.120; -; 1.
DR Gene3D; 3.30.420.360; -; 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; 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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000003560};
KW Transferase {ECO:0000313|EMBL:EEA90834.1}.
FT DOMAIN 3..100
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT DOMAIN 235..435
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT REGION 439..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
SQ SEQUENCE 1042 AA; 109883 MW; 4B081AA5AFE06089 CRC64;
MKHARIHITG IVQGVGMRPF VYRQATEHGV TGWVLNAGDG VHIEAHAEGG ALEAFVHSLR
DQAPAAAQVD TVDVAFFDKA EEPIVEPDAS TLEPAADVRP GAEAVHPLQA EPRFRIIASQ
DETEHSTLVS PDIATCDDCL RELFDPSDRR YHYPFINCTN CGPRFTIIRG LPYDRAQTSM
GAFPMCPACA SEYADPLDRR FHAQPDACFA CGPHITWQER GGREALVGAT RETSDAIIAR
CAELIASDGI VAIKGLGGFH LACRADSERA VRELRARKRR SNKPLAIMAR DLDAAGALCH
VGPKERDLLY GSIKPIVLLQ RRGSMSGENP PSSSGLASSV AFDLPELGIM LPYTPLQHLL
MAECRVRGID ALVMTSGNLS EEPIEMDNGA AWARLVESGI ADALLGNDRA ILSRFDDSVV
RAVNGQVQFV RRARGYAPRP LALPNSEGHG AARRTQDTRP AREAEGADAK ATILPTSPYE
ASPTTPPAGT PGASSLSLAA GPAASAPTGP SGYEPRDNRP LCVLACGPEQ KATLALTRED
GTGGAQCFIS QHIGDLENAE TFDAWQSARA RMEGLFDLRP SALTCDVHPG YLSSQWAREQ
ARATGLPLVQ VQHHHAHIAA VIAEAAARGE IEANARVIGI AFDGTGAGAV YNSDSQNSGI
VRPGSDSNTE AACHNGVQTG SACRDIRTAA SETPADGVKA RVPKLNIADM TPDAGAANRP
LELDGTIWGG EVLLASLSSF DRAAHLEPWP LPGGAASVRD PRRNAFALLK HYDLLDHPGA
APLLDTLQPD EKELASRMIE RGINCPLTSS MGRLLDAVSA ILGICHSATY EGEPAILLEA
AAHRFTRHYG AVGSSVIVAK SLDAQKSLVV PKSPSAPNGS GVPNGLTTPN DPGDPNGPTA
QDSPAAPKSP DTPGLPATPT DNEPLGKSLP STATSISMQP LLLHILDGIA QGASPEQLAW
DTHRAIVEIT ARTAVEISNS TGVRTAALSG GVFMNRLLLE GISVELERAG LTVLTPRDLP
CNDGGIAYGQ AAVARALLNG QG
//
