ID A0A1S8C7E8_9ACTN Unreviewed; 481 AA.
AC A0A1S8C7E8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acetyl-/propionyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:OMQ14479.1};
DE Flags: Fragment;
GN ORFNames=A7K94_0216325 {ECO:0000313|EMBL:OMQ14479.1};
OS Modestobacter sp. VKM Ac-2676.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1678130 {ECO:0000313|EMBL:OMQ14479.1, ECO:0000313|Proteomes:UP000093049};
RN [1] {ECO:0000313|EMBL:OMQ14479.1, ECO:0000313|Proteomes:UP000093049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2676 {ECO:0000313|EMBL:OMQ14479.1,
RC ECO:0000313|Proteomes:UP000093049};
RA Vasilenko O.V., Tarlachkov S.V., Ariskina E.V., Ariskina K.I., Avtukh A.N.,
RA Evtushenko L.I.;
RT "Draft genome sequence of Actynobacteria Modestobacter sp. strain VKM Ac-
RT 2676.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMQ14479.1}.
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DR EMBL; MBFF02000650; OMQ14479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8C7E8; -.
DR Proteomes; UP000093049; 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 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; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 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:UP000093049}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 481
FT /evidence="ECO:0000313|EMBL:OMQ14479.1"
SQ SEQUENCE 481 AA; 51535 MW; 6A2A24BBCEAAC05B CRC64;
MQKVLIANRG EIAVRVARAC RDAGLTSVAV YAEPDRDALH VRAADEAFAL GGTTPGDSYL
VVDKILDAAR ASGADAVHPG YGFLSENADF ARAVIDAGLT WIGPSPQAIV DLGDKVAARH
IATRAGAPLV PGTKDPVADA DEVVAFAREH GLPVAIKAAF GGGGRGLKVA RTLEEIPELF
DSAVREAVAA FGRGECFVER FLDRPRHVEA QVLADTHGTV VVVGTRDCSL QRRNQKLVEE
APAPFLTDEQ RERIHSSAKA ICREAGYHGA GTVEYLVGTD GSISFLEVNT RLQVEHPVTE
ETSGIDLVRQ QFRIAEGLPL EITEDPTPRG HSIEFRINAE DAGRNFMPAP GPVTRLEVPQ
GPGVRWDSGV EAGGEVAGAF DSMLAKLIVT GATRTEALQR ARRALDELVV EGMPTVVPFH
RAVVRDPAFT SEPFTVHTRW IETGWDNQVP PYSAAPAAGD EQEPRQTVVV EVGGRRLEVS
L
//
