ID H3K930_9FIRM Unreviewed; 474 AA.
AC H3K930;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Acetyl-CoA carboxylase, biotin carboxylase subunit {ECO:0000313|EMBL:EHR35582.1};
GN ORFNames=HMPREF9454_01753 {ECO:0000313|EMBL:EHR35582.1};
OS Megamonas funiformis YIT 11815.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Megamonas.
OX NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR35582.1, ECO:0000313|Proteomes:UP000005963};
RN [1] {ECO:0000313|EMBL:EHR35582.1, ECO:0000313|Proteomes:UP000005963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR35582.1,
RC ECO:0000313|Proteomes:UP000005963};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Megamonas funiformis YIT 11815.";
RL Submitted (JAN-2012) 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:EHR35582.1}.
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DR EMBL; ADMB01000079; EHR35582.1; -; Genomic_DNA.
DR RefSeq; WP_008539219.1; NZ_JH601091.1.
DR AlphaFoldDB; H3K930; -.
DR STRING; 437897.GCA_900128435_01251; -.
DR GeneID; 69725718; -.
DR PATRIC; fig|742816.3.peg.1697; -.
DR HOGENOM; CLU_000395_3_2_9; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000005963; 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 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; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..440
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..311
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 474 AA; 52579 MW; 7D16F85E206CDCBB CRC64;
MFKRVLIANR GEIAVRIIRA CQEMGIETVA VYSDEDADAM HVRLADYSYN IGPADASESY
LNIDALMEAA ERTEADAVHP GYGFLSEDAD FAEMVTKAGM TWIGPWADTI RKVGDKDEAR
AAMIPSGIPM SKGSTPLTSV EDAVEQAKDV GYPIILKPVA GGGGKGMLIA NSEDDLRNIL
TIIDINKVKY YFEHYIEHSR HIEVQIVADN YGHVIHLGER ECSLQRRNQK LLEESPSIAL
TPDRRAEVGA LAIKAAKSVH YNNIGTVEFL LDLKTNQFNF MEINPRIQVE HGVTEAVTGI
DLVRTQIRIA AGESLDLQQE DVKFTGHAIE CRINAEDPDN NFMPSPGKID FFLEPGGPRV
RVDSGVCAGL SISPYYDSLI AKIVVRGRTR GDAIKIMRRA LNEFKVGGIK TTIPLHQRIL
KNEYFCTGDI DTRFIRNHFS KYVQPMTPAQ LKASKTAKTE KEIINAINAS MYYA
//