ID A0A2P6TKL5_CHLSO Unreviewed; 2644 AA.
AC A0A2P6TKL5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:PRW44840.1};
GN ORFNames=C2E21_6288 {ECO:0000313|EMBL:PRW44840.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW44840.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW44840.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC {ECO:0000256|ARBA:ARBA00003838}.
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the nitrate reductase family.
CC {ECO:0000256|ARBA:ARBA00006253}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRW44840.1}.
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DR EMBL; LHPG02000012; PRW44840.1; -; Genomic_DNA.
DR SMR; A0A2P6TKL5; -.
DR STRING; 3076.A0A2P6TKL5; -.
DR OrthoDB; 167515at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR CDD; cd18316; BTB_POZ_KCTD-like; 1.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.60.40.650; -; 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; 2.
DR Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_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; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00174; Oxidored_molyb; 2.
DR Pfam; PF00645; zf-PARP; 1.
DR PRINTS; PR00363; CYTOCHROMEB5.
DR PRINTS; PR00407; EUMOPTERIN.
DR SMART; SM00225; BTB; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50064; ZF_PARP_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 134..247
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 1027..1102
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 1559..1778
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1563..1608
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 2258..2333
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 2371..2519
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 394..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2102..2146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2227..2253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2290..2317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2334..2381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2512..2612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2582..2597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2644 AA; 280152 MW; 5A16A8514F491501 CRC64;
MLARSLGASV HCSAGAGSQQ PAPRPARALK ALPKGLGAAA ALLAARPALA AEPFGSDGIG
GSSIELPSLP ALPAVELPSV DVSALGLDSI DPLYVAAGAA LVAIPLGLGA LLGGGNTPRA
KAVPAATAVE ALAADPGCLL VDIRSKAEAA EVGSPSLKGV SKRAPAAVPF IAVSKEGDVI
VDVAFGEKVA KLKGVDDLSK PLILIDTDGS LSPAAAKIVL KELPDKSVYF ITGGTDAWQE
AGFPWKEPLR FALPDFSNID LSNIDLTAGI NTVVGGAKAL ADDFAEAPSV TKGILAAGAV
AGASVLLFSQ AELLFEVAGL FAAGQFLFKM LFAEEREKAL TEIKKVAEQV DIEDLPEDLG
KIATTLLEDK TGTQVIGREG AAAGAADSAA AASASSTPAP GAAAPPTPVP VTPAPAASAA
SGSGASASAS APVEPVPSAA KSDMAEDVVA AYAGALFIRS EAEIKRPVVL LSGERTNVFG
VLEKHFCETA LPPSERFWRA VRTRWTPALE TWRPRVNGVQ LKVLAGARLP ESEEEWAALR
TAMTGVRQHL RSDTSVELLL SDLKDFVAMV VSWWENRKKT ENGGAAASLQ LMKRVASAGM
LLGSFPLGKR PCLEYMHLAA AAHHDQLLHH PPGPLPGSYA AGGCGGSAHG GTYYATPEIV
SVPLLAGGGS GHLPPLRRDG AGGAPVVFEE LPQHNSNPAV HGGGGYMQQL AGNSEAELFG
ELFPGGGDAG TAAVGRGSQS PRDQLAGPQG GSGFLPPLAT GLANGGGYAQ QSPRDRREGS
AENKEPALPA LPTPPAADGG GSSADSGKRP VALNVGGFSF LTTAATLAAV DGSYFCKLAR
QTARASGGGA AEFFIDRSGK AFEYVLDYLR ARRFTDPAPS ALPREERALE LLAREADFYA
LPELAARART ALAQLQQPAA TADETPSDVP AAAALEGSVR NGQLLGSLAA APQLARVSGS
GSPAAVLDAV FLETGFQPAA TLGEAQAALL QQLNAMIQAK QGDGFSVVDF KCGTERDGTL
RNLHYHYKVQ ESPSGRAKCQ ACKEAIAKGA LRLGVLIEHP DYGEWWIWRH WECVTDRVVK
NMEHPSNLEG LDDLPKEYQD MVHATFGNPP APKPRKQKVK KEDGGEAAAA EVAPVAATGS
KGKSKSKGKS KRGAASLGDT VDAEVALPAA AEEQAEADPL EYLREDLGQM LTLMMGGVLP
EVMVPFFAPE GAYRGRLSVL ISELQTSGVL ASPWPTPAHD YQMHTQYEAA QAAAAQEAAA
GKKRPKRRTR RPRGYDSDGD WRGMEGQVEE RPVQASPPAK EVDEEPNLDS AQKPRKRLKK
QAAAGEQGGA SDKQRRKGAD DKPKKKRKQR RESAAEWELP LAGRWERRPD PLEPYRQQLK
DELMERFRDK MPKEFNGYFR REDPWELGPL IPQLQMPVAC PSEGFNAPIG DVCLQLWSGS
RPCLRTLGGE LLKKNAFMEE LGLEDVPARS LVVVQRRPDG GWQQLGTINT LTKQPQLAHW
QAPAAGHAAL GAPARSPLKM AAPAQLVQAR GSSTRRRSLL ACPACKSVRR GAAAGEAAEA
LACPVCYCEA DEEPQGHTHL DCGHPYCNAC LANYLHSAYQ GGTHPKCQKP GCEQLLSEED
LQQGVLVLCD CPDVRQQRSA ARLPPLDDPL AAYQRFTALA AAALAREGGD LIECQRCHFM
ILVEEDAPED APCPNCRRGK PLLEARQAAE CPRGIQQVEG ERVLYCPSCA FGPQQKAMHC
NKLKCGGCGL LLCWCCGEVI GEQRVYDHFA DDKCPLYGLP GERPEMTAAE QEAAQERAVQ
REAYYQQMWD LIVHPAHRAV RGMRRATPPD MQADDALWQR VHNVMHSRLE RAFNEITEAA
AAREEQLPVL ELQAQLLPRA GTLLDAAWPG WDVWEGVVDE RDKGTPDEWI RRNPDMIRLT
SKHPLNAEPP LSQLLEAGFH TPTALHYVRN HGAVPLIHWE DHRLEVAGLV ERPCQLSMDE
LAQRFPQHSV LATLSCAGNS GPEGEVAGGD GTYATSVPLW KGLDPLSEVV LAWKHNGRLL
QPDHGYPLRV VIPGYIGGRC VKWLTRIELS AGWWSLPEFV CYNLNIGSVI AAPAHDEVIN
LPPASGGGGS GGGTEAAGDG SGSGKGAEGG AAGGKGEQGG GQEKEEPSYT LRGFAHTGAG
HLVIRVELSF DGGSSWHQAH IADREPGNSH FIVKIRKQET PDGTRQLRFL HPVANGRDSG
GWMVEEKQAA GEAEGGAPSE QMEEEEAAAQ AGKAWDSLRS ISWDEIKQHT SRESCWFVRD
GRVYDPTQFL DKHPGGPSAI LSNAGQDASA EFDPIHSGDA RRMTLEYLIG KVEGADPPFK
PGRRKAEPGG PAAAPAAGAA GEGGEGDEPA LQKGKARLTE KEEITHDTRR FRFALPREGQ
RLGLPVGHHI TVTAQLKGEK VVRPYTPEGD PIDVRGPWGE FHYLGAGRFT YKGREGHCRR
INLLGGGTGI TPLYQVMRAI MEDENDPTEM CLVFANKTPQ DVLLRRRLQR ASEEHAFPPG
NEDGGGAYGS SGGEGSAVGK AGDSKDSGSS SGGAEGQTEE ADGGDAEQGG KADGGNEQTG
GKQGGDDGSS SQDGGGKSGS KPHKDSPESC GTIALICGPP PMVEKACLPA LRELGFDEDH
IIVF
//
