ID A5AZP7_VITVI Unreviewed; 891 AA.
AC A5AZP7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=riboflavin kinase {ECO:0000256|ARBA:ARBA00012105};
DE EC=2.7.1.26 {ECO:0000256|ARBA:ARBA00012105};
GN ORFNames=VITISV_023071 {ECO:0000313|EMBL:CAN78503.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN78503.1};
RN [1] {ECO:0000313|EMBL:CAN78503.1}
RP NUCLEOTIDE SEQUENCE.
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT vinifera L.): coping with a highly heterozygous genome.";
RL PLoS ONE 2:e1326-e1326(2007).
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000256|ARBA:ARBA00005201}.
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DR EMBL; AM441561; CAN78503.1; -; Genomic_DNA.
DR UniPathway; UPA00276; UER00406.
DR ExpressionAtlas; A5AZP7; baseline.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd22160; F-box_AtFBL13-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.40.30.30; Riboflavin kinase-like; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR023468; Riboflavin_kinase.
DR InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF82114; Riboflavin kinase-like; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 729..867
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 99966 MW; F96D22FB4815F6A3 CRC64;
MESEPEESHS SESEGSLISE QEEGSYSSES EGSHSSESEG NDGYYSSHDS GANQSVRGDD
DEDDGDEEIS SRKDGISELS DSILIRILSF LPMKYVVATS ILSKRWQFLW TMVPNLVFRF
RRRDEHFVNS IDKTLVLHQN SQIKKFLIDF TYQSQFQSSV NVWIRHATRK NVEELHLQFR
VGQHIRSSPM DYAHALPQFL YANSSIVKLS LWFCNIKPTW VISWPSLKTL SIGSVELCDD
LIEEILSGCP ALESLELHHC FGINSLNITS ASLKKLVINR YWDSSHSHHR SVLKISAPNV
QSLGILGNMY TKECRVKNVP SLFDASLNFE LAMQEGNPKD HYKLYHKVVM KLLKSVNHVK
ALTVGTWCIQ ISVEVGFSFT DLHNFDEEKY WSSREGVLAN SLINLKTVKI IGVIWNQPGI
ELVFGLVLTI MQALFKTTYL CKRFGLTLQV HAGAFLNWSF EISVENGRII SVESPCLVFK
MSAAKPLKKL VSGVILDLDG TLLNTDGIVS EVLKVFLVKY EKQWNGKVAH KLIGKTPFEA
AAVIVEDYGL PCTTEELMSE ITPMFSNQWC NIKALPGANR LIKHLHGHGV PIALASNSPR
ASIESKISCH QGWKESFSVI IGGDEVRMGK PSPEIFLEAS KRLSVKPSNC LVIEDSLPGV
MAGKAAGMEV VAVPSIPKQS HIFNSADEVI NSLLDLRPEX WGLPSFQDCK PLRYFLSYSQ
TFPRVEDTLP VEPWYIGGPV IKGFGRGSKV LGVPTANLST EGYSTLLSEQ SSGVYFGWAG
LSKQGVYKMV MSIGWNPYFN NTEKTIVSAT WTVKEPWLLH EFDEDFYGEE LHLVIVGYIR
PEANFSSLES LIAKIHEDRR IAERALDLPL YSNFKDDPYL KIPLHGVKNH S
//
