ID A0A3D8MAS0_9ALTE Unreviewed; 669 AA.
AC A0A3D8MAS0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acetyl/propionyl/methylcrotonyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:RDV27464.1};
GN ORFNames=DXV75_05395 {ECO:0000313|EMBL:RDV27464.1};
OS Alteromonas aestuariivivens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1938339 {ECO:0000313|EMBL:RDV27464.1, ECO:0000313|Proteomes:UP000256561};
RN [1] {ECO:0000313|Proteomes:UP000256561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52655 {ECO:0000313|Proteomes:UP000256561};
RA Zhang J., Du Z.-J.;
RL Submitted (AUG-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:RDV27464.1}.
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DR EMBL; QRHA01000003; RDV27464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8MAS0; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000256561; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000256561}.
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 584..665
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 669 AA; 73479 MW; 972394A99CD7527D CRC64;
MIDKLLIANR GEIACRIIRT ARKIGIATVA VYSDADASAL HVALADESIH IGSPPAKESY
LAADKIIAAA RKLGANAIHP GYGFLSENAD FARLCENNQI IFVGPPAAAI EAMGSKSAAK
KIMQKAGVPL IPGYHDNDQS DTALQKAAQE MGYPVLLKAS SGGGGKGMRQ VWRQEDFTAA
LEAARREALA SFGDDAMLVE KYLTRPRHVE VQIFCDQHGQ GVYLFERDCS VQRRHQKIIE
EAPAPGLGAA LRKQMGETAL RAAQAIDYVG AGTVEFLLDE DGQFYFMEMN TRLQVEHPVT
EKITGEDLVE WQLRVAEGAP LPKSQQQLTA KGHAFEARIY AEDPANGFLP STGRLKMLQP
PEEDTHTRVD TGVQEGDEVS VFYDPMIAKL VVWDENRDKA LQRLLSALQQ YYVDGVTTNI
PFLYSVAASE PFRSARLVTT FIDLYQDQLL PGRPELAEDT LAIMALLEML NRQRGSTINR
EDPHSPWSLQ NAWRANEVHC QQLRLTAGNQ EFELYITPSK GIEPAPGSWQ VQYRQQVWQV
SGSLEGHYIH AIINGHRSRV AWSGNEQGFV IFTAGHALRF AAVTPDLGDT EIAGANPSFQ
APMNGTIVKL TAEPGEQVKA GATLMIMEAM KMEHCITAPV DGKVKQYFFA AGDLVDGGTT
LLEYEPYEA
//
