ID V9KPJ0_CALMI Unreviewed; 525 AA.
AC V9KPJ0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Cytochrome b5 reductase 4 {ECO:0000256|ARBA:ARBA00022339};
DE EC=1.6.2.2 {ECO:0000256|ARBA:ARBA00012011};
DE AltName: Full=Flavohemoprotein b5/b5R {ECO:0000256|ARBA:ARBA00031842};
DE AltName: Full=cb5/cb5R {ECO:0000256|ARBA:ARBA00030883};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFP00589.1};
RN [1] {ECO:0000313|EMBL:AFP00589.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFP00589.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00029341};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000256|ARBA:ARBA00006105}.
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DR EMBL; JW868071; AFP00589.1; -; mRNA.
DR AlphaFoldDB; V9KPJ0; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 2.60.40.790; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR007052; CS_dom.
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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR PANTHER; PTHR19370:SF185; NADH-CYTOCHROME B5 REDUCTASE 2; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51203; CS; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 55..131
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 170..261
FT /note="CS"
FT /evidence="ECO:0000259|PROSITE:PS51203"
FT DOMAIN 278..389
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 59578 MW; 1355BFEBC429B51B CRC64;
MLRPPTQAFP AAASQQRLSG GTDRNKVQLK PGRSLMDWIR LTKSGKDLTG LKGRLIEVPE
EELAKHNKKD DCWICIRGMV YNLTPYLEYH PGGEEELMRG AGIDGTELFD QIHRWVNYES
MLKECLIGRM ALKPASINKV SDRSRVKMST RTLLNGASVP GAGFEKTLRD VSLRYEWFQT
EDAVTVVIYT KQKDINSDSV IIDLAEGVLR TEVRLEESSY VFHMKLSHEV QEVVSVHCAN
TVGKIELCMK KADNTMWSDL GLPLENHDSR KKNSDRGLFY RKCKLLSKTD VTHDTRLLCF
QLPLGCHLTV PIGQHIYLKN SIHDTEVVRP YTAALPSLYP EPEDNSHILT NIYLMIKIYP
HGVFTPFIDS LQIGDSVSVS NPEGSFRCSQ MKGKAELLLL AAGTGFTPMI NVIRFALKES
CCLRKIRLIF FNKKEEDILW RDQLDQLSSK DNRFEVDYIL SDPHPEWTGK RGRIEMSHCS
ELRSKCTEES KTLVCVCGPA SFTELAFGFF KQIGFSDEEI HAFNG
//
