ID F2K2J3_MARM1 Unreviewed; 594 AA.
AC F2K2J3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Oxaloacetate decarboxylase alpha subunit {ECO:0000313|EMBL:ADZ90038.1};
DE EC=4.1.1.112 {ECO:0000313|EMBL:ADZ90038.1};
GN OrderedLocusNames=Marme_0755 {ECO:0000313|EMBL:ADZ90038.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90038.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ90038.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
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DR EMBL; CP002583; ADZ90038.1; -; Genomic_DNA.
DR RefSeq; WP_013659943.1; NZ_CP047696.1.
DR AlphaFoldDB; F2K2J3; -.
DR STRING; 717774.Marme_0755; -.
DR KEGG; mme:Marme_0755; -.
DR PATRIC; fig|717774.3.peg.786; -.
DR eggNOG; COG0511; Bacteria.
DR eggNOG; COG5016; Bacteria.
DR HOGENOM; CLU_000395_4_3_6; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000001062; Chromosome.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005776; OadA.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01108; oadA; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Lyase {ECO:0000313|EMBL:ADZ90038.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001062}.
FT DOMAIN 8..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 516..594
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 594 AA; 63984 MW; 74A7185DDAACE05A CRC64;
MTTTKQPLGI TDVVLRDAHQ SLFATRLRID DMLPIAEKLD KVGFWSLESW GGATFDSCIR
FIGEDPWDRI RELKKAMPNT PQQMLLRGQN LLGYRHYADD VVAKFVERAA TNGVDVFRIF
DAMNDPRNLE QAIKSVKEVG KHAQGTLSYT KSHVHTTKTW VDYAKTLEDM GADSIAIKDM
SGILTPYDAF ELVGLLKEQT DLEVQLHAHA TSGLSDMTIL KAVEAGIDRV DTAISSMSMT
YGHSATESVV AALQGTNRDT GLDLALLEEI AAYFRVVRKK YAKFEGSLRG TDSRILIAQV
PGGMLTNMEN QLKEQGAADK FDEVLEEIPK VRQDLGMIPL VTPTSQIVGT QAVLNVLTGE
RYKSISKETA GVLKGEYGAA PAEFNKELQT RVLDGAEPIT CRPADLLEPE VEKLTQELET
LASEKGIALS NESIDDVLTY ALFPQIGLKF LENRGDASAF EPVPTGEELV AKAPVEAGPA
VYTVSVSGQS YVVEVTDGGD ISQIQPVGSA SAAPVAAAAP APASGGEDVP APLAGNIFKV
LVSPGQQVQE GETIMILEAM KMETEISAPK SGVVGSIYVK EGDAVQVGQA LVSL
//