ID A0A1E3QZ59_9ASCO Unreviewed; 1434 AA.
AC A0A1E3QZ59;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=BABINDRAFT_57000 {ECO:0000313|EMBL:ODQ82911.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ82911.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
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DR EMBL; KV454426; ODQ82911.1; -; Genomic_DNA.
DR RefSeq; XP_018988239.1; XM_019132270.1.
DR STRING; 984486.A0A1E3QZ59; -.
DR GeneID; 30150123; -.
DR OrthoDB; 5474937at2759; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR Pfam; PF01855; POR_N; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000094336}.
FT DOMAIN 677..826
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 1434 AA; 156289 MW; 8DE48A1943D9A5C2 CRC64;
MIILGKEIDL NLFKEAGSAL NKAPAVSQAE AVSHVANAAG GVNFTTQTAK AVESAFALTD
THKLVGANDA FAVIADYLTT EQPALATVAT TGAALLQNLP FLNQTAFKNR SVVIHAQLTA
DFSPVTSLRD LGLPILVSQT AQEAQDLALV AYAYAAHAQT TVLHFFAPSE AQKFNLIDSA
AVQKFIQATA SSEKIIDEDA QFDTLASLLH NVGKYKPYET VSTAKNPTDA IFLLGEASES
LSKAVHADGS SILLSIRLYR PISVAQVLAS LPLSVKTLTV VEQSSHTQQF SPLLLDLFAD
SAKLFDRGLT KVVSTNFGVV SDHAVAVATV LGNTRAEKPI QNLTVGAAEQ VCGADVAAAQ
AQAQTLESAY ITMLQQVNDR LTILNAQSSD SIGDAANPEF GYGAFLNGEE QKKSLVGLVQ
EAVRASVFSA SLTKRLSEWL VQGKTDSAAI ISALEAEADE SKTAILALSS HFTESSSWIV
GSDSWSYDLG SSGVHHLVSS GKNLNMLIID SEPQATDRKV NGFRKKDVGL YAMNFGGCYV
ASVAVYASYT QVLQAFIEAE KFEGPSIVMA YLPYHSESDD TLAVLQETKR AVDSGYWPLY
RYSPNETEPF KLDSSSLKKE LKDFLDRENK LTLLALKNPV LARTLVASQT NDVKEKQEAK
AKEAYAQLLE GLSGPPVTVA FASDGGNAEG LAKRIGRQAL GRGLKATVLA MDDIPIEDLS
AEENVIFVTS TAGQGEFPQN GKTLWDGLKG SLDLDLTGVN FSVFGLGDSQ YWPRKEDAHY
YNKPCKDLFA KLAFFGAGEI APLGLGDDQD ADGYSTGYNV WIEQIWEGLG VAGLAGVEEP
KPLTNEDMKL GSDYLRGTIV EGLQDQSTGA ISAVDQQLTK FHGIYMQDDR DVRDQRKADG
LEPAYSFMVR VRLAGGVSTP QQYLKMDELS NTRGNGTLKV TTRATFQLHG VVKHDLKPAI
RGMNAALMDT LAACGDVNRN VMCSALPGNR KVHSQINEAS KIISEHLLPQ TTAYHEIWLE
GADAGDKPGD SAVWENRVEG PTKKKTLVAG NALADVEPMY KNLYLPRKFK IVITVPPFND
VDVYAHDIGL IAIVNESDVV IGYNVLAGGG MGTTHNNKKT YPRAGSMMGY CSADKIHIAC
EKIMLVQRDN GDRTNRKHAR LKYTIDDMGV EAFKTAVEEY WGERFEAPRE FEIKSNIDYF
GWAQDETGLH HFTCFIENGR IEDTPELPQK QGLKEIAEYM VEKKFGNFRL TGNQHFLISD
ITDEHLDHVK GLMKKYKLDN TNFSALRMGS SACVAFPTCG LAMAESERYL PVLVSKLEGA
LEEYGLRHDS VTMRMTGCPN GCARPWLAEV ALVGKAFGAY NLLLGGGYHG QRLNKIYRYS
IKEDEILDTL KPLFKRWALE RHEGEHFGDF VIRVGVIKPT LEGKYFHDDI PEEA
//