ID A0A0E3W2W3_9FIRM Unreviewed; 559 AA.
AC A0A0E3W2W3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-grasp fold {ECO:0000313|EMBL:CFX26532.1};
GN ORFNames=877 {ECO:0000313|EMBL:CFX26532.1};
OS Syntrophomonas zehnderi OL-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX26532.1, ECO:0000313|Proteomes:UP000045545};
RN [1] {ECO:0000313|EMBL:CFX26532.1, ECO:0000313|Proteomes:UP000045545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX26532.1,
RC ECO:0000313|Proteomes:UP000045545};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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; CGIH01000013; CFX26532.1; -; Genomic_DNA.
DR RefSeq; WP_052729596.1; NZ_CGIH01000013.1.
DR AlphaFoldDB; A0A0E3W2W3; -.
DR STRING; 690567.877; -.
DR Proteomes; UP000045545; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
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; PTHR48095:SF5; BLL7292 PROTEIN; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000045545}.
FT DOMAIN 2..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 476..550
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 559 AA; 61016 MW; AB0A7D7F20590EB5 CRC64;
MRMKNILIAN RGEIAIRIAR AAADLGLGAV AVYSADDDRS LHRRIADRSY ALTGRGAGAY
LDLEQIIIAA KDTNCDAIHP GYGFLSENAT FARRCAEEGL TFIGPRPDLL ELFGDKTAAR
SFAKRCGVPL LPGSAGPVSL EEAREFFLTL GRDASVMIKA TLGGGGRGMR PVYKLADLDE
AYARCQSEAR SAFGLGDVYI EKLIRQPRHI EVQVIGDGKQ VIHLGERDCT MQRRSQKIIE
VAPSKALTPQ LRDKITTAAL RLAQEAHFLS LGTIEFLLEG NGGDEALFAF MEVNPRLQVE
HTITEEITGI DLVRAQIEIA AGKSLAELGL TDDVPRPRCY AMQLRINMET IDSTGLANPT
TGTLNSYEIP SGPGIRVDGY GYNGYTNNPA FDSLLAKLIV TSRSPHYQDV VTKAYRALQE
FKIEGIETNI PFLLNLLRRP EMLENNYHTR FIEENASELV SADRPVEDFS ASNPSTAPEG
TVALKAPVLG RIVDIAVNVG DLVTEGQIVV VMEAMKMEYE VQAEQSGYVM AVNVVQDDVV
SSGDPLIFIA AADRFRHVS
//
