ID A3XF80_9RHOB Unreviewed; 250 AA.
AC A3XF80;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 03-MAY-2023, entry version 66.
DE SubName: Full=Propionyl-CoA carboxylase, alpha subunit {ECO:0000313|EMBL:EAQ43525.1};
GN ORFNames=MED193_21746 {ECO:0000313|EMBL:EAQ43525.1};
OS Roseobacter sp. MED193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ43525.1, ECO:0000313|Proteomes:UP000005943};
RN [1] {ECO:0000313|EMBL:EAQ43525.1, ECO:0000313|Proteomes:UP000005943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ43525.1,
RC ECO:0000313|Proteomes:UP000005943};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ43525.1}.
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DR EMBL; AANB01000016; EAQ43525.1; -; Genomic_DNA.
DR AlphaFoldDB; A3XF80; -.
DR STRING; 314262.MED193_21746; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_5_5; -.
DR Proteomes; UP000005943; 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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 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..250
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..211
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 250 AA; 26865 MW; 4BF018A14DD790E1 CRC64;
MFEKILIANR GEIACRVIKS ARKMGIKTVA IYSDADKQAL HVQMADEAVH IGPPPANQSY
IVIDKVMEAI RATGAQAVHP GYGFLSENSK FAEALATEGV AFVGPPVGAI EKMGDKITSK
KIAKEAGVST VPGHMGLIED ADEAVKISQE IGYPVMLKAS AGGGGKGMRI AWNDEEAREG
FQSSKNEAAN SFGDDRIFIE KFVTQPRHIE IHCFATPMAM ALPGRARVLD PASSAESCRR
ARALSWMRPP
//
