ID   A0A024GDM3_9STRA        Unreviewed;       871 AA.
AC   A0A024GDM3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-NOV-2023, entry version 28.
DE   RecName: Full=Phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN9_056870 {ECO:0000313|EMBL:CCI44863.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI44863.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI44863.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI44863.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
CC       {ECO:0000256|ARBA:ARBA00010995}.
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:CCI44863.1}.
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DR   EMBL; CAIX01000081; CCI44863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024GDM3; -.
DR   STRING; 65357.A0A024GDM3; -.
DR   InParanoid; A0A024GDM3; -.
DR   OrthoDB; 9826at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR13158; -; 1.
DR   PANTHER; PTHR13158:SF5; NAD KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   ACT_SITE        58
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        148
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         57..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   871 AA;  99788 MW;  AE3656622FA82A9D CRC64;
     MFWSALLSQK AIPGMRQSSR STSLLRYHVL HASTGPLGSD DDAPLPVPRL KELVLIRHGE
     SEGNVARQKS LQGDDSLFYG EFKNRHSSNW RLTDRGRQQA LAAGEWLREN NLVHFDRYFV
     SEYLRAMETA SRLQLPDAKW YAEMLLRERD WGQMDLMSEQ ERISTMQHEL QRRDLDRFYY
     APPGGESLAA VAQRVDRLFC SLNRECNAKK AIVVCHGEVI WAMRTRLERM SQDTFRELQD
     SGRMVDQIHN GHILHYTRTD PFTGEVAPSF SYMRSVCPWN EKLSPKGWIK IERPVYDNEM
     LLAIAERVPR MIVSEEYIEE TYKRAKSSFM IPKAARAEQS ITSSIAMNTL MASTSQNAPS
     DVKPMYNSAK KALDLKKVLV VNKMTRFEHE CELHGNSGDA LRKQMSMRGF VYDRLKASHD
     HHVEALEDIT STLKQHSIQV DVISADRLNH EAVNSADMVF SAGGDGTFLK AASFVNTPIP
     VAGLNTDPVR SEGKLCCYAV DQVCNRFSTV LERLLEGKFN WRLRQRIRVG MVNQDGFWYE
     LPRYALNEVF IAESDASRPS HYNIGVDQHQ RESQRSSGII VCTGTGSSAW YYSACQMYRE
     QVAKVLQAMH HTHTNETVTE LTELFNKESV YSEDSVDLGY IVREPIINET FGDIRFRRGK
     ARRVSMRSLG WDMRVTLDGI YSVPLDYGVQ AVMKVCDEPK YVLRTVDFSD SYGETSKESY
     WCSLLSPSIK SKLKFAHKVS EPALEMPLDA QEKSQEGLDQ QLKCLKYELE LLSSTSDRIS
     QLLAVLTEEQ RQLLYAKKRL QSSVKAGQQT HSTRLIRIRD EQKIRMQIAQ EKAIMQSQNL
     AKLRESQLQV RLETNESESD VSGLLEQEFE M
//