ID Q6N6S5_RHOPA Unreviewed; 671 AA.
AC Q6N6S5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Acyl-CoA carboxylase biotin-carrying subunit {ECO:0000313|EMBL:CAE27980.1};
DE EC=6.3.4.14 {ECO:0000313|EMBL:CAE27980.1};
GN OrderedLocusNames=RPA2539 {ECO:0000313|EMBL:CAE27980.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE27980.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE27980.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; BX572601; CAE27980.1; -; Genomic_DNA.
DR RefSeq; WP_011158089.1; NZ_CP116810.1.
DR AlphaFoldDB; Q6N6S5; -.
DR STRING; 258594.RPA2539; -.
DR GeneID; 66893602; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_5; -.
DR PhylomeDB; Q6N6S5; -.
DR Proteomes; UP000001426; Chromosome.
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 CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
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; 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; 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:CAE27980.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001426}.
FT DOMAIN 10..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 129..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 592..667
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 671 AA; 71554 MW; AEE17D95F95719C2 CRC64;
MMKSPALYRR FRTLLIANRG EIACRVIRTA RAMGLRTVAV YSEADVGAQH VAEADEAVLL
GPARARDSYL NIERIIQAAK QTGAEAVHPG YGFLSESAEF AQACADAGLV FVGPTPQMIT
AMGSKSGSKA LMEKAGVPLV PGYHGAAQDE ATLAAAADKI GFPVLVKASA GGGGRGMRVV
REAGELAAAI VSAKREAKAA FGDDTLLIER YVDNPRHIEV QIVGDSHGNL VSLFERECTL
QRRHQKVIEE APSPTLDAAQ RETVCAAARR AAGAVNYVGA GTIEFVSDGK DVFFIEMNTR
LQVEHPVTER ISGVDLVEWQ LRVAFGEALP LKQDQLKLSG HAIEARVYAE NPAKNFMPSV
GKITTWRTPA EVDGLRIDAG YRGGDSVSPY YDAMLAKVIA WAPTRQAAID RLDRGLNETD
VRGVVTNIPF LSALVTHPEV RANAIDTGFI ERNLAALTAA PSTLGDLEFA AAVAAILRGE
DEAAKAEGPS PWRTAGWMPV GRRKRSFLFR RGQGHDHTDH TIELTYGGGS SALTIDGREL
AFAWTAAGDG IDVALGDARS RIHAVVDGAE LYVRTRSGRF ELHLVDPFGG ESEEAVGEDK
IVAPLPGTVV ALLAEVGAKL DKGAPILTLE VMKMEQTLRA PFAGTLTAVK CKVGDIVQEG
AELAELEADA D
//
