ID A0A425XXA3_9BACT Unreviewed; 658 AA.
AC A0A425XXA3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 10.
DE SubName: Full=ATP-grasp domain-containing protein {ECO:0000313|EMBL:RRG19276.1};
GN ORFNames=DWB61_16005 {ECO:0000313|EMBL:RRG19276.1};
OS Ancylomarina euxinus.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Ancylomarina.
OX NCBI_TaxID=2283627 {ECO:0000313|EMBL:RRG19276.1, ECO:0000313|Proteomes:UP000285794};
RN [1] {ECO:0000313|EMBL:RRG19276.1, ECO:0000313|Proteomes:UP000285794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1P {ECO:0000313|EMBL:RRG19276.1,
RC ECO:0000313|Proteomes:UP000285794};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Ancylomarina sp. M1P.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:RRG19276.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QQWG01000022; RRG19276.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A425XXA3; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000285794; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 2..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 580..657
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 658 AA; 74572 MW; C403E8F99718A581 CRC64;
MYYKRLLIAN RGEIAVRIIR TAHKLGISTL VIYSDKDKEA DHVRLADEAY PLKGDDLLST
YLDKQQIIKI AVENKADAIH PGYGFLAENP EFAKACSEAN IDFVGPDAKS IELMGNKVNA
REFAVLQNLP VLEGIIGDKA TLLKNSSQLQ FPILVKAAAG GGGKGMRIVR AESDLESAIL
ATSREAEKYF GDGEVLLERY IENPRHIEVQ VLADKHGNAI HLFERECSIQ RRFQKIIEEA
PSASVSPELR QRMGNAAVRL TQALGYSNAG TIEFLMDENN AFYFLEMNTR IQVEHPVTEM
ITGIDLVEEQ LAIASGKKLR YKQGDIVLNG HAIEARIYAE DPEQDFIPAP GYVEFYREPV
VTNTKLRVDS SLSDASMIYP DFDPMISKLI VWDESRDLAI EGLKQALSDY HIHGIKNNIH
FLKNLIGTDE YNQNQISTHF CKDNEKELLV RMNQDQQSID HALFYAAFSH FDLQIDQAKN
IWEEIGYWRN ARKAFKLTHD DKTIEVISRD KMTYEIDSKP YRFEKLELNN NCINLIHKGK
IYSFYISKDE RNEAHISCKG ILVSLRRWSD SVNELFNESF EEVGKSGDRI LAPLPGKVVK
INVKLGEKIQ KSDVLLILES MKMENSILAP FDAVVSEIVI KEGEQVKSQM ELIKLIEA
//
