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Database: UniProt
Entry: A0A2I0M2Z4_COLLI
LinkDB: A0A2I0M2Z4_COLLI
Original site: A0A2I0M2Z4_COLLI 
ID   A0A2I0M2Z4_COLLI        Unreviewed;       767 AA.
AC   A0A2I0M2Z4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Hexose-6-phosphate dehydrogenase (Glucose 1-dehydrogenase) {ECO:0000313|EMBL:PKK24042.1};
GN   Name=H6PD {ECO:0000313|EMBL:PKK24042.1};
GN   ORFNames=A306_00006122 {ECO:0000313|EMBL:PKK24042.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK24042.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK24042.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK24042.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC       {ECO:0000256|ARBA:ARBA00004959}.
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:PKK24042.1}.
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DR   EMBL; AKCR02000044; PKK24042.1; -; Genomic_DNA.
DR   STRING; 8932.A0A2I0M2Z4; -.
DR   InParanoid; A0A2I0M2Z4; -.
DR   UniPathway; UPA00115; -.
DR   Proteomes; UP000053872; Unassembled WGS sequence.
DR   GO; GO:0017057; F:6-phosphogluconolactonase activity; IEA:InterPro.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   CDD; cd01400; 6PGL; 1.
DR   Gene3D; 3.40.50.1360; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR019796; G6P_DH_AS.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR01198; pgl; 1.
DR   PANTHER; PTHR23429:SF7; GDH_6PGL ENDOPLASMIC BIFUNCTIONAL PROTEIN; 1.
DR   PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   Pfam; PF01182; Glucosamine_iso; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..767
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014144446"
FT   DOMAIN          29..211
FT                   /note="Glucose-6-phosphate dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00479"
FT   DOMAIN          224..500
FT                   /note="Glucose-6-phosphate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02781"
FT   DOMAIN          536..758
FT                   /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT                   /evidence="ECO:0000259|Pfam:PF01182"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10005"
SQ   SEQUENCE   767 AA;  86643 MW;  3D2F8498091992E5 CRC64;
     MLRRVLCAVL FVGTLPSLAK GSQGHISVVL LGATGDLAKK YLWQGLFQLY MDQVSSGHSF
     TFHGAALTAL EPGQRLMFDV LKKLACPPDE APNRCAVLKD QFLKLSQYHQ LKTAENYTAL
     NREIETLLRQ EGLKEAGRIF YFSVPPFAYT EIARHINSSC RPPPGAWLRV VLEKPFGHDL
     ESAQQLAAEL TSFFREEEMY RVDHYLGKQA VAHILPFRDQ NRQFLDPIWN XXXLKETVDA
     RGRTSFYEQY GVIRDVLQNH LTEALMFLTM ELPANVSRAE EVLQCKLQAF QSLRRLEKSS
     AVLGQYQAYA SQVQDELQKA QDYISTTPTF AGVLVHSDNL RWEGVPFLLT SGKALDERVG
     YVRVLFKNRA YCTQSETLRD AGHSQCKAKQ IIFYIGHGAL NTPAVLVSRN LFRPVMPEGS
     WREAVGQSDL HIFGQPLSDY YVYRPVKERD AYSVLISNIY HGRKDFFITT ENLLASWAFW
     TPLLDSISYQ PLRLYPGGVE NQHLLDFEMV SGEVAFTVAE TIQSKFRQSP LVSAWSEDLI
     SQLASDIEKT ARRTVAHSGQ FHLALSGGSS PVVLFQRLAR HHYTFPWKHT HIWLVDERCV
     PLTDTESNFF SLHNHLLQNI RVPYFNVHPM PVHLNQRLCV EEDRGTELYA KEIVALVANA
     SFDLVLLGVG SDGHTASLFP RSDNGLEGVQ AVVLTESPVK PHQRMSLSLP LINKARQVFV
     LVLGKGKHDI TTLLSRVGHE PRKWPVSGVS PSSGQLVWYV DYEALLG
//
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