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Database: UniProt
Entry: H3K930_9FIRM
LinkDB: H3K930_9FIRM
Original site: H3K930_9FIRM 
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
//
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