ID A0A0X3VWE9_9ACTN Unreviewed; 635 AA.
AC A0A0X3VWE9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Acety-l/propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:KUL48572.1};
GN ORFNames=ADL22_09250 {ECO:0000313|EMBL:KUL48572.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL48572.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL48572.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL48572.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL48572.1}.
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DR EMBL; LLZI01000087; KUL48572.1; -; Genomic_DNA.
DR RefSeq; WP_066975650.1; NZ_LLZI01000087.1.
DR AlphaFoldDB; A0A0X3VWE9; -.
DR STRING; 1609095.ADL22_09250; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000053256; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 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; PTHR18866:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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:UP000053256}.
FT DOMAIN 2..435
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 98..309
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 557..634
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 635 AA; 66535 MW; 5D7195A605A1576B CRC64;
MEIRSVLVAN RGEIARRIFR TCRELGIATV AVHSDADADA AHVRDADAAV RLPGDAPAAT
YLRGDLIVRA ALAAGADAVH PGYGFLSESA AFAAQVADAG LIWIGPPPAA IEAMASKTRA
KELMAAAGVP LLAPVDPAAA TAADLPLLLK AAAGGGGRGM RIVRELDALA GELASARAEA
AAAFGDGEVF AEPYVEGGRH VEVQVLADAH GAVWTLGTRD CSLQRRHQKV IEEAPAPGLP
AALRETLHRS AAQAARAIGY RGAGTVEFLV SADGRAYFLE MNTRLQVEHP VTEEIYRIDL
VALQIAVAEG RPLPAALPEP HGHAVEARLY AEDPAAGWQP QTGTVHRLTV PGGVRLDSGV
DDGDTVTVHY DPMLAKVIAW APTRAEAVRK LAGALERARI HGPVTNRDLL VSSLRHPEFA
AATGLDTGFY DRHLAALTGS GEADASGGAL SALAAALADA HGRSRFGGFR NVPSGPQHKR
YACGGTVHDV RYRLGRDGLT AEDFPGVRLL ALSGERVVLE VDGVRRPFAV ARYRDRVHVD
SPLGARAFTA LPRFPDPAAR TEPGSLLAPM PGTVVRIADG LAEGDRVEAG RPLLWLEAMK
MEHRITAPAA GTLTALPVRT GQQVEVGTLL AVVTA
//
