KORA_MYCTU
ID KORA_MYCTU Reviewed; 653 AA.
AC O53182; F2GHL4; L0TCE2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2-oxoglutarate oxidoreductase subunit KorA;
DE EC=1.2.7.3 {ECO:0000269|PubMed:19936047};
DE AltName: Full=Alpha-ketoglutarate oxidoreductase subunit alpha/gamma;
DE Short=KG oxidoreductase subunit alpha/gamma;
DE Short=KGO subunit alpha/gamma;
DE Short=KOR subunit alpha/gamma;
GN Name=korA; OrderedLocusNames=Rv2455c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ROLE IN TCA CYCLE, GENE NAME,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19936047; DOI=10.1371/journal.ppat.1000662;
RA Baughn A.D., Garforth S.J., Vilcheze C., Jacobs W.R. Jr.;
RT "An anaerobic-type alpha-ketoglutarate ferredoxin oxidoreductase completes
RT the oxidative tricarboxylic acid cycle of Mycobacterium tuberculosis.";
RL PLoS Pathog. 5:E1000662-E1000662(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Component of KG oxidoreductase (KOR) that catalyzes the CoA-
CC dependent oxidative decarboxylation of 2-oxoglutarate (alpha-
CC ketoglutarate, KG) to succinyl-CoA. Methyl viologen can act as electron
CC acceptor in vitro; the physiologic electron acceptor is unknown. Is
CC involved in the alternative TCA pathway that functions concurrently
CC with fatty acid beta-oxidation. Since a growing body of evidence
CC indicates that lipids (for example cholesterol and fatty acids) are a
CC predominant growth substrate for M.tuberculosis during infection, flux
CC through KOR likely represents an important step in intermediary
CC metabolism in vivo. KOR-dependent decarboxylation of KG also appears to
CC be an important source of CO(2) in M.tuberculosis metabolism.
CC {ECO:0000269|PubMed:19936047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2
CC + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + succinyl-CoA;
CC Xref=Rhea:RHEA:17297, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57292; EC=1.2.7.3;
CC Evidence={ECO:0000269|PubMed:19936047};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000269|PubMed:19936047}.
CC -!- SUBUNIT: KG oxidoreductase (KOR) is composed of KorA and KorB subunits.
CC {ECO:0000269|PubMed:19936047}.
CC -!- DISRUPTION PHENOTYPE: CoA-dependent KG oxidoreductase activity is
CC absent in a mutant strain deleted for both genes korA and korB, and
CC this strain is impaired for aerobic growth in the absence of sufficient
CC amounts of CO(2). Inhibition of the glyoxylate shunt or exclusion of
CC exogenous fatty acids alleviates this growth defect. Simultaneous
CC disruption of korAB and kgd results in strict dependence upon the
CC glyoxylate shunt for growth. {ECO:0000269|PubMed:19936047}.
CC -!- MISCELLANEOUS: Is extremely stable under aerobic conditions.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45248.1; -; Genomic_DNA.
DR PIR; F70864; F70864.
DR RefSeq; NP_216971.1; NC_000962.3.
DR RefSeq; WP_003412627.1; NZ_NVQJ01000024.1.
DR AlphaFoldDB; O53182; -.
DR SMR; O53182; -.
DR STRING; 83332.Rv2455c; -.
DR PaxDb; O53182; -.
DR DNASU; 887370; -.
DR GeneID; 45426445; -.
DR GeneID; 887370; -.
DR KEGG; mtu:Rv2455c; -.
DR PATRIC; fig|83332.111.peg.2748; -.
DR TubercuList; Rv2455c; -.
DR eggNOG; COG0674; Bacteria.
DR eggNOG; COG1014; Bacteria.
DR InParanoid; O53182; -.
DR OMA; LNPFPKN; -.
DR PhylomeDB; O53182; -.
DR BioCyc; MetaCyc:G185E-6687-MON; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.920.10; -; 1.
DR InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR InterPro; IPR033412; PFOR_II.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR Pfam; PF17147; PFOR_II; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF01855; POR_N; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
DR SUPFAM; SSF53323; SSF53323; 1.
DR TIGRFAMs; TIGR03710; OAFO_sf; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..653
FT /note="2-oxoglutarate oxidoreductase subunit KorA"
FT /id="PRO_0000420516"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 653 AA; 69182 MW; B15D0DF492C2DBC5 CRC64;
MDPNGSGAGP ESHDAAFHAA PDRQRLENVV IRFAGDSGDG MQLTGDRFTS EAALFGNDLA
TQPNYPAEIR APAGTLPGVS SFQIQIADYD ILTAGDRPDV LVAMNPAALK ANIGDLPLGG
MVIVNSDEFT KRNLTKVGYV TNPLESGELS DYVVHTVAMT TLTLGAVEAI GASKKDGQRA
KNMFALGLLS WMYGRELEHS EAFIREKFAR KPEIAEANVL ALKAGWNYGE TTEAFGTTYE
IPPATLPPGE YRQISGNTAL AYGIVVAGQL AGLPVVLGSY PITPASDILH ELSKHKNFNV
VTFQAEDEIG GICAALGAAY GGALGVTSTS GPGISLKSEA LGLGVMTELP LLVIDVQRGG
PSTGLPTKTE QADLLQALYG RNGESPVAVL APRSPADCFE TALEAVRIAV SYHTPVILLS
DGAIANGSEP WRIPDVNALP PIKHTFAKPG EPFQPYARDR ETLARQFAIP GTPGLEHRIG
GLEAANGSGD ISYEPTNHDL MVRLRQAKID GIHVPDLEVD DPTGDAELLL IGWGSSYGPI
GEACRRARRR GTKVAHAHLR YLNPFPANLG EVLRRYPKVV APELNLGQLA QVLRGKYLVD
VQSVTKVKGV SFLADEIGRF IRAALAGRLA ELEQDKTLVA RLSAATAGAG ANG
