ID A0KVT3_SHESA Unreviewed; 674 AA.
AC A0KVT3;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE SubName: Full=3-methylcrotonoyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:ABK47902.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:ABK47902.1};
GN OrderedLocusNames=Shewana3_1669 {ECO:0000313|EMBL:ABK47902.1};
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122 {ECO:0000313|EMBL:ABK47902.1, ECO:0000313|Proteomes:UP000002589};
RN [1] {ECO:0000313|Proteomes:UP000002589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3 {ECO:0000313|Proteomes:UP000002589};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK47902.1; -; Genomic_DNA.
DR RefSeq; WP_011716699.1; NC_008577.1.
DR AlphaFoldDB; A0KVT3; -.
DR STRING; 94122.Shewana3_1669; -.
DR KEGG; shn:Shewana3_1669; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR OMA; LVKWQLM; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000002589; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
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; 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; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; PS00866; CPSASE_1; 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, ECO:0000313|EMBL:ABK47902.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 589..666
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 674 AA; 73521 MW; 545D05C9FEDB83D6 CRC64;
MLTKLLIANR GEIACRIIKT AQAMGVRTVA LYSDADKNAR HVAMADESFY LGGSAPADSY
LKGDLIIEIA KKAQAQAIHP GYGFLSENAD FARKCEAAGI VFVGPGSDAI DAMGSKSAAK
AIMTAAQVPL VPGYHGDDQT DATLKAEALK IGFPMLIKAA YGGGGKGMRI VEHEGEIMDA
INSARREAAS SFGNDKLLME RYLRQPRHVE VQVFADTFGN AIYLSDRDCS IQRRHQKVVE
EAPAPGLSDE LRTQMGEAAV AAAKAIDYVG AGTVEFLLDT DNSFYFMEMN TRLQVEHPVT
EMVTGQDLVK WQLMVASGQP LPLKQDEVRI HGHAFEVRIY AEDPQNEFLP ASGKLNFLRE
PEQSKYVRID SGIRENDVIS NFYDPMIAKL IVWDESRPRA LQRLVHALES YQISGLKHNI
EFLANIAEHP AFAKADFSTD FINRYGDALI SSASSETDTA LAFAALYQVL ARKEAAKAQA
INSADPYSPW GQVSGFRLNS VSQHSIALLD DAHELQQLVL LDFGDHYQLS QPTADGQVSK
SLSGELKQDL LLAEINGHKS KVPVSAQGDD FTLFLPSGSY HFRAVKTQVV EAESSNEDKL
KAPMNGTVVT HLVEVGAEVN AGQGLLVMEA MKMEYTIEAP FDGIVTEFYF KAGELVSDGA
VLLHVEPKAQ SEEA
//