ID R4M2Z5_MYCTX Unreviewed; 302 AA.
AC R4M2Z5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Hemoglobin-like protein {ECO:0000313|EMBL:AGL25125.1};
GN ORFNames=I917_25090 {ECO:0000313|EMBL:AGL25125.1};
OS Mycobacterium tuberculosis str. Haarlem/NITR202.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=1304279 {ECO:0000313|EMBL:AGL25125.1, ECO:0000313|Proteomes:UP000013563};
RN [1] {ECO:0000313|EMBL:AGL25125.1, ECO:0000313|Proteomes:UP000013563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Haarlem/NITR202 {ECO:0000313|EMBL:AGL25125.1,
RC ECO:0000313|Proteomes:UP000013563};
RX PubMed=23788533;
RA Narayanan S., Deshpande U.;
RT "Whole-Genome Sequences of Four Clinical Isolates of Mycobacterium
RT tuberculosis from Tamil Nadu, South India.";
RL Genome Announc. 1:e00186-13(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP004886; AGL25125.1; -; Genomic_DNA.
DR KEGG; mtuh:I917_25090; -.
DR PATRIC; fig|1304279.3.peg.5098; -.
DR HOGENOM; CLU_003827_14_1_11; -.
DR BioCyc; MTUB1304279:G13AB-3394-MONOMER; -.
DR Proteomes; UP000013563; 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 GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
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:ARBA00022714}.
FT DOMAIN 1..67
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 213..302
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 302 AA; 32139 MW; 290188C839FDE8CD CRC64;
MTLRVPSERT GSVARCYSLX SSPYTDDALA VTVKRTADGY ASNWLCDHAQ VGMRIHVLAP
SGNFVPXTLD ADFLLLAAGS GITPIMSICK SALAEGGGQV TLLYANRDDR SVIFGDALRE
LAAKYPDXRS LVLHWLESLQ GLPSASALAK LVAPYTDRPV FICGPGPFMQ AARDALAALK
VPAQQVHIEV FKSLESDPFA AVKVDDSGDE APATAVVELD GQTHTVSWPR TAKLLDVLLA
AGLDAPFSCR EGHCGACACT LRAGKVNMGV NDVLEQQDLD EGLILACQSR PESDSVEVTY
DE
//
