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Database: UniProt
Entry: A0A1E4TT39_PACTA
LinkDB: A0A1E4TT39_PACTA
Original site: A0A1E4TT39_PACTA 
ID   A0A1E4TT39_PACTA        Unreviewed;       490 AA.
AC   A0A1E4TT39;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Cytochrome b2, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PACTADRAFT_50736 {ECO:0000313|EMBL:ODV94884.1};
OS   Pachysolen tannophilus NRRL Y-2460.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Pachysolen.
OX   NCBI_TaxID=669874 {ECO:0000313|EMBL:ODV94884.1, ECO:0000313|Proteomes:UP000094236};
RN   [1] {ECO:0000313|Proteomes:UP000094236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-2460 {ECO:0000313|Proteomes:UP000094236};
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=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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DR   EMBL; KV454015; ODV94884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4TT39; -.
DR   STRING; 669874.A0A1E4TT39; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000094236; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02922; FCB2_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF149; L-LACTATE DEHYDROGENASE (CYTOCHROME); 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094236}.
FT   DOMAIN          1..75
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          107..463
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
SQ   SEQUENCE   490 AA;  54977 MW;  66199AD64AC2A1D4 CRC64;
     MPTVEEVKTH DNEEDCWIII HGKAYNVTDF LDEHPGGKDI ILKYAGRDAT KAFDVVHPRD
     MVDHLAEENH LGDVEGDMEA VAPDDADEED EQTEEEIKRQ ELISLKPDLS KILNLFDFEL
     VARQIMTNNG WAYYSSGADD EITLRENHLA YQQIFFRPRI LINVSNVDLS TTMLGCPSKL
     PFYVTATALG KLGHADGEKI LTRACGTSGI IQMIPTLASF SFDEIADEAI DGQNQWFQLY
     VNSDRKVTER IVRHAEERGI KGLFITVDAP ALGRREKDMR SKFSSDQDSN VQKINEKESK
     QIDRNQGAAR AISSFIDTSL NWEDIKWFQS ITKMPIILKG VQRWEDAVRA AEIGCSGIVI
     SNHGGRQLEF APAPVEVLAE IEKFLIFVDG GIRRATDIMK ALSLGCNGVG IGRPFLYAMS
     TYGQEGVEKA FDILRDELEM NMRLIGATKI DDLNESFVNI KGTGKRTIPN DYLFNSVYEP
     LGSSNFKPKL
//
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