ID A0A1G9VFN3_9ACTN Unreviewed; 613 AA.
AC A0A1G9VFN3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:SDM70871.1};
GN ORFNames=SAMN04487981_102333 {ECO:0000313|EMBL:SDM70871.1};
OS Streptomyces sp. cf386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDM70871.1, ECO:0000313|Proteomes:UP000198720};
RN [1] {ECO:0000313|Proteomes:UP000198720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; FNHV01000002; SDM70871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9VFN3; -.
DR STRING; 1761904.SAMN04487981_102333; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000198720; 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; 3.40.50.20; -; 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; 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:UP000198720}.
FT DOMAIN 1..424
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 97..299
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 534..611
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 613 AA; 65604 MW; 04FF145FB40FA19D CRC64;
MITSVLVANR GEIACRIFRT CGELGIRTVA VYSDADANAL HTRVADAAVR LPGAAPSVTY
LDGDLIVKAA VAAGADAVHP GYGFLSENAD FARAVLDAGL VWIGPPPEAI EAMASKTRAK
ELMGLAPLGE VTEADLPVLV KAAAGGGGRG MRVVRRPEEL SDALEGARAE AASAFGDGEV
FVEPYIENGR HVEVQILADT HGTVWALGTR DCSLQRRHQK VIEESPAPGL TERLTDELHT
LAVRAARAVD YVGAGTVEFL VAGDKAHFLE MNTRLQVEHP VTEAVFDIDL VAEQLRVAEG
HALADEPPHA RGHAVEARLY AEDPARDWAP QTGTLHRFAV PEGVRLDTGF TDGDEIGVHY
DPMLAKLIAH APTRAGAIRK LAGALERSTL HGPLTNRDLL VRSLRHEEFT SARMDTAFYD
RHLTDLTDPA PDPYAPLAAA LADAHGRSRF AGWRNVPSQP QTKRYAMAGE EIEVRYRHTR
AGLEADGVRI VHADAALVVL EADGVRRNFE VARYGDEIHV NATRLTALPR FPDPTEQHTP
GSLLAPMPGT VVRVAEGLAV GAPVRAGEPL LWLEAMKMQH KIAAPVTGTL TALHAVPGLQ
VTVGALLAVV QET
//
