ID A0A370X9A4_9GAMM Unreviewed; 667 AA.
AC A0A370X9A4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:RDS84851.1};
GN ORFNames=DWU98_02530 {ECO:0000313|EMBL:RDS84851.1};
OS Dyella monticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1927958 {ECO:0000313|EMBL:RDS84851.1, ECO:0000313|Proteomes:UP000254258};
RN [1] {ECO:0000313|EMBL:RDS84851.1, ECO:0000313|Proteomes:UP000254258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G-K06 {ECO:0000313|EMBL:RDS84851.1,
RC ECO:0000313|Proteomes:UP000254258};
RA Gao Z., Qiu L.;
RT "Dyella monticola sp. nov. and Dyella psychrodurans sp. nov. isolated from
RT monsoon evergreen broad-leaved forest soil of Dinghu Mountain, China.";
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:RDS84851.1}.
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DR EMBL; QRBE01000001; RDS84851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370X9A4; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000254258; 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; 3.30.700.40; -; 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; 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; IPR048429; MCC_alpha_BT.
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 Pfam; PF21139; MCC_alpha_BT; 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; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 588..664
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 667 AA; 73360 MW; 63ED2A40A6281742 CRC64;
MFERVLIANR GEIACRVIRT CRRLGIRTIA VYSEADRDAQ HVRLADEAWP IGGSRPAESY
LRGDVILDVA KKSGAQAIHP GYGFLSENTA FARACADAGV TFIGPRPESI DAMGSKAAAK
ALMEHHQVPL VPGYHGDNQD TGFLTEQARK TGFPLMIKAA AGGGGKGMRI VRTEKEFADA
LASAQREAAS SFGDTRVILE RYVEHPRHIE FQVFGDTHGN LIHLNERECS AQRRYQKVLE
ETPSPFLNET RRNAMGEAAV AAAKAVDYVG AGTVEFIVAQ DGTFYFMEMN TRLQVEHPVT
EETLGLDLVE WQLRVAAGES LPLRQDEIHA RGHAIEVRLY AEDPDQNFLP GSGTLRCLRL
PRPSDHVRLD GGVVEGDTVT IFYDPMIAKL IVHDTDRTQA LQRLREALAE CDIVGPKSNI
AFLERLSRHP VVVEGCIDTG YLDRHLDEFL TGDAAPSADV LFAAATAALL RDERAVLEST
ACVSDPHSPW SRADAWRIGH AGKRIVALSL REQRYEVQAY GHDGDYRLQH DASHCQVHGA
RYEADVLSAR FDDRSMRLRV HADQERIALH DTDGQRYTFS RAAAFAWESK GGAGGHQVIA
PMPGRIVLVK AKAGDNVEEG QELLVMEAMK MELALKAPRA GTIEVISAMQ GEFVEADAVL
VRFTSSS
//
