ID A0A0G3IV62_9MYCO Unreviewed; 566 AA.
AC A0A0G3IV62;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Chemotaxis protein CheY {ECO:0000313|EMBL:AKK29141.1};
GN ORFNames=AB431_23450 {ECO:0000313|EMBL:AKK29141.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK29141.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK29141.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK29141.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000849};
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DR EMBL; CP011773; AKK29141.1; -; Genomic_DNA.
DR RefSeq; WP_047331956.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3IV62; -.
DR STRING; 1545728.AB431_23450; -.
DR KEGG; mye:AB431_23450; -.
DR PATRIC; fig|1545728.4.peg.4768; -.
DR Proteomes; UP000035237; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT DOMAIN 12..135
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 69
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 566 AA; 61398 MW; 3864CB5C405C68A1 CRC64;
MTGPAPQPRK PVILTVDDDP AVSRAVARDL RRHYGERYRI VRAESGLDAL ETINELKLRG
ETVAVFVADY RMPQMSGIQF LEEAMDVYPM ARRVLLTAYA DTHAAIDAIN VVDLDHYLLK
PWDPPEEKLY PVIDALLEAW HATGDRAIPH TKVIGHRWSE RSWEVRQFLA RNLHSFRAFN
ADEPKGKQLL DAGGLDDFEL PVVISEQGQI MVNPTDAELA AMLGLSTSPS LEMYDLAVIG
GGPAGLAAAV YGASEGLKTV LIEETTTGGQ AGRSSRIENY LGFPTGVSGA ELTTSARRQA
ERFGAEVITT RRAIKLSAGE SGTARTIEFE DGTTIAARAV ILATGVAYRQ LQVTGCWDNP
DDPSCNYVGR GVYYGASVSD ASECRGEDVY IVGGANSAGQ AAMFMSREAR SVTMLVRGPS
LEASMSHYLI QQIEKNPTIT VRTCTEVVDT LGEDDHLTGL VLENRQTGQR ETVEAGRMCC
FIGAEPRTDW LKEVVAVDDH GFVLAGPDLL NVAGWTLDRP PHHLETSVPG VFVAGDVRSE
SAKRVAAAVG EGSMAVMLVH RYLAEA
//
