ID B2HIY4_MYCMM Unreviewed; 673 AA.
AC B2HIY4;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Electron transfer protein FdxB {ECO:0000313|EMBL:ACC43447.1};
GN Name=fdxB {ECO:0000313|EMBL:ACC43447.1};
GN OrderedLocusNames=MMAR_5043 {ECO:0000313|EMBL:ACC43447.1};
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43447.1, ECO:0000313|Proteomes:UP000001190};
RN [1] {ECO:0000313|EMBL:ACC43447.1, ECO:0000313|Proteomes:UP000001190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000854; ACC43447.1; -; Genomic_DNA.
DR RefSeq; WP_012396567.1; NC_010612.1.
DR AlphaFoldDB; B2HIY4; -.
DR STRING; 216594.MMAR_5043; -.
DR KEGG; mmi:MMAR_5043; -.
DR eggNOG; COG1018; Bacteria.
DR eggNOG; COG3239; Bacteria.
DR HOGENOM; CLU_003827_14_0_11; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd03514; CrtR_beta-carotene-hydroxylase; 1.
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; IPR005804; FA_desaturase_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
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; PF00487; FA_desaturase; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000001190};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..430
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 584..673
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 75332 MW; C59AFF663ABDD5C0 CRC64;
MSTIDAVNRA APDSSAHHAL PDPGETVPKL ALPTLGIFLA ALGSFVLTTV GYIDGWVPFW
VTIPVNAAVT FVMFTVVHDA SHYSVSSVRW VNGLFGRLAF LFVGPVVAFP AFGYIHIQHH
RHSNDDVEDP DTFASHGSPW LLPLRWSLVE YYYLKYYIPR ARSRPVVEFA ETLFMFALSI
TGLTIAIVTG NFWTLAVVFL IPQRIGLTVL AWWFDWLPHH GLEDTQRTNR YRATRNRVGA
EWLFTPVLLS QNYHLVHHLH PSVPFYRYVR TWKRNEEAYL ERNAAISTVF GQQLNPDEYR
QWKELNGRLA KLLPVRMPAR SSSPHAVLHR IPVASVDPIT TDSTLVTFAV PEDLQDAFRF
EPGQHVTVRT DLGGQGVRRN YSICAPATRA QLRIAVKHIP GGAFSTFVAN DLKAGDVLEL
MTPTGQFGTP LNPLERKHYV GLVAGSGITP VLSILATTLE IEAESRFTLI YGNRTKESTM
FRAELDRLES RYADRLEILH VMSNEPLHTP ELRGRIDTEK LNRWLTSNLS PETVDEWFIC
GPMEMTTTVR DSLIEHGVDT EHIHLELFFG YNTAPATDHG YEGATVTFTL SGRQDTFDLT
PGDSILEGAL QRRSDAPYAC MGGACGTCRA KLIEGNVEMD HNFALGQAEL DAGYILTCQS
HPTTPFVAVD YDS
//
