ID G2G9J4_9ACTN Unreviewed; 614 AA.
AC G2G9J4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Propionyl-CoA carboxylase alpha chain {ECO:0000313|EMBL:EGX59773.1};
GN ORFNames=SZN_10823 {ECO:0000313|EMBL:EGX59773.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX59773.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX59773.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX59773.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) 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:EGX59773.1}.
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DR EMBL; AGBF01000024; EGX59773.1; -; Genomic_DNA.
DR RefSeq; WP_007494175.1; NZ_AGBF01000024.1.
DR AlphaFoldDB; G2G9J4; -.
DR PATRIC; fig|700597.3.peg.2113; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000004217; 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:UP000004217}.
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 614 AA; 64984 MW; 1125B90D25AA1F4B CRC64;
MITSVLVANR GEIACRVFRT CRAAGIRTVA VYADADAGAL HTRAADTAVR LPGAAPSDTY
LRGDLIVRAA LTAGADAVHP GYGFLSENPG FARRVLDAGL TWIGPSPEAI EAMASKTRAK
ELMGVEPLRE VTEADLPVLV KAAAGGGGRG MRVVRRLADL DAALDGARAE ARGAFGDGEV
FVEPYLEDGR HVEVQILADT HGTVWVLGTR DCSLQRRHQK VIEEAPAPGL PPELTASLHE
MAVRAARAVG YTGAGTVEFL VAAGDAHFLE MNTRLQVEHP VTEAVYGVDL VALQIRVAEG
HALDEAPPPA RGHAVEARLY AEDPARDWAP QTGTLHRLAV PGGIRLDSGF TDGDEIGVHY
DPMLAKAVAH APTRAEAVRA LAGALERAAV HGPPTNRDLL VRSLRHEEFT TARMDTGFYG
RHLAELTEPA PDPLAPLAAA LADAHGRSRF GGFRNLPSRP QTKRYLLAGE ETEVRYHHTR
AGLAADGVRV VHADAALVVL EADGVRRTFE VARYGDEIHV NADRLTALPR FPEAAAQHAP
GSLLAPMPGT VVRVAEGLTE GSAVEAGQPL LWLEAMKMEH RISAPASGTL SALHAAPGRQ
VTVGALLAVV QPAP
//
