ID Q3YS51_EHRCJ Unreviewed; 533 AA.
AC Q3YS51;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Transcriptional regulator, BadM/Rrf2 family {ECO:0000313|EMBL:AAZ68454.1};
GN OrderedLocusNames=Ecaj_0411 {ECO:0000313|EMBL:AAZ68454.1};
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68454.1, ECO:0000313|Proteomes:UP000000435};
RN [1] {ECO:0000313|Proteomes:UP000000435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; CP000107; AAZ68454.1; -; Genomic_DNA.
DR RefSeq; WP_011304532.1; NC_007354.1.
DR AlphaFoldDB; Q3YS51; -.
DR STRING; 269484.Ecaj_0411; -.
DR KEGG; ecn:Ecaj_0411; -.
DR eggNOG; COG1104; Bacteria.
DR eggNOG; COG1959; Bacteria.
DR HOGENOM; CLU_003433_0_0_5; -.
DR InParanoid; Q3YS51; -.
DR Proteomes; UP000000435; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.50; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR030489; TR_Rrf2-type_CS.
DR InterPro; IPR000944; Tscrpt_reg_Rrf2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00738; rrf2_super; 1.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF02082; Rrf2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
DR PROSITE; PS01332; HTH_RRF2_1; 1.
DR PROSITE; PS51197; HTH_RRF2_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 164..515
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 533 AA; 59400 MW; FB87D6950FFEFFA9 CRC64;
MLITTRLRYA VMFMVSLAQE YYILKGSNQP KKMSHIADSQ SLSEGYLEQI IAKLKKQGLV
NSTKGPGGGY FLNKSPNIIT LNLILESIGE NIKITRCKNN NVIRCLPNNA KCITHNLWDN
IGNYIKKYLN SISLEDIINN NFKHSIKHSI KHSNILNNDE NKYIYADYNS TSTILPVIKQ
QLDNLSSLNI YNPSSTHKLG QNTRSIIEKT REIAINILNA RNYDVIFTSS GTEANNLVIN
STTEYKHLIS SIEHVSIMNC TTDAELIPVN SNGVICLDRF SETLNKFKDK KVLVSIMTAN
NETGVIQPIK EIVEISHKFG ALVHTDAVQA CGKIHIDIEN LGVDLLTISS HKLGSIAGTG
VLFFNSKKIK IKPMILGGNQ EKGLRAGTEN IISIYLLSIS LNNLKDSIKK MSTVEKLRDK
LEYEILNLVP EAQIFGKNTQ RLPNTTCISM PNVSSEIQTI SFDIENIAVG NGSACSSGTL
TRSHVLSAMG IDDDIAKNSI RISLSPDITE HQIKKIVNCW YKTYQNNKLL KLK
//
