ID S9YL24_CAMFR Unreviewed; 2680 AA.
AC S9YL24;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|RuleBase:RU000485};
DE EC=1.1.1.44 {ECO:0000256|RuleBase:RU000485};
GN ORFNames=CB1_000455014 {ECO:0000313|EMBL:EPY84700.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY84700.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY84700.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC Evidence={ECO:0000256|RuleBase:RU000485};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3. {ECO:0000256|ARBA:ARBA00004874, ECO:0000256|RuleBase:RU000485}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|RuleBase:RU000485}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; KB016740; EPY84700.1; -; Genomic_DNA.
DR UniPathway; UPA00115; UER00410.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd22727; FHA_KIF1B; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR CDD; cd01233; PH_KIFIA_KIFIB; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006183; Pgluconate_DH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR049780; PH_KIFIA_KIFIB.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR NCBIfam; TIGR00873; gnd; 1.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00461; 6PGD; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW ECO:0000256|RuleBase:RU000485};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW NADP {ECO:0000256|RuleBase:RU000485};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Oxidoreductase {ECO:0000256|RuleBase:RU000485};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU000485};
KW Reference proteome {ECO:0000313|Proteomes:UP000030684}.
FT DOMAIN 42..350
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 529..585
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 2072..2170
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 879..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1922..1941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1994..2031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 648..675
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 835..869
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1009..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2680 AA; 300822 MW; 539C60B8D6DE6A7C CRC64;
MGREGACWMP ASCGKAGVGS ALGSSGLLWQ PYWEDDLTNP LGAKSGCWKA PSDSPGSFQG
IINPKNPKEA PKSFSFDYSY WSHTSPEDPC FASQNRVYND IGKEMLLHAF EGYNVCIFAY
GQTGAGKSYT MMGKQEESQA GIIPQLCEEL FEKINDNCNE EMSYSVEVSY MEIYCERVRD
LLNPKNKGHL RVREHPLLGP YVEDLSKLAV TSYTDIADLM DAGNKARTVA ATNMNETSSR
SHAVFTIVFT QKKHDSETNL STEKVSKISL VDLAGSERAD STGAKGTRLK SKKKKKTDFI
PYRDSVLTWL LRENLGGNSR TAMVAALSPA DINYDETLST LRYADRAKQI KCNAVINEDP
NAKLVRELKE EVTRLKDLLR AQGLGDIIDN LKDFQNSKHR YLLASENQRP GNFSTASMGS
LTSSPSSCSL NSQVGLTSVT SIQERIMSTP GGEEAIERLK ESEKIIAELN ETWEEKLRKT
EAIRMESPLR DVRSKLIICN HFQTPHLVNL NEDPLMSECL LYYIKDGITR VGQADAERRQ
DIVLSGAHIK EEHCIFRSER NNSGDVIVTL EPCERSETYV NGKRVAQPVQ LRSGNRIIMG
KNHVFRFNHP EQARAEREKT PSAETPSEPV DWTFAQRELL EKQGIDMKQE MEKRLQEMEI
LYKKEKEEAD LLLEQQRLDA DSDSGDDSDK RSCEESWKLI TSLREKLPPS KLQTIVKKCG
LPSSGKKREP IKMYQIPQRR RLSKDSKWVT ISDLKIQAVK EICYEVALND FRHSRQEIEA
LAIVKMKELC AMYGKKDPNE RDSWRAVARD VWDTVGVGDE KIDDMMASSK GGTDVDDLKV
HIDKLEDILQ EVKKQNNMKD EEIKVLRNKM LKMEKVLPLI GSQEQKTQGN HKAKEPVGAG
ASSKSENDVS KGDSGELGKE ERVSQLMNGD PAFRRGRLRW MRQEQIRFRN LQQQEIAKQL
RRQNVPHRFI PPENRKPRFP FKSNPKHRNS WSPGTHIIIT EDEVIELRIP KDEDARKGNK
EESQEKGSRA ASKDPQLPWG SQGIRSQDHI QVSKQHINNQ QQPPQLRWRS NSLNNGQPKS
TRCQASASSE SLNSHSSHPT ADLQTFQAKR HIHQHRQSYC NYNTGVPWTQ QEFELAQWAF
RKWKSHQFTS LRDLLWGNAV YLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPELLPTEM
EKTHEDRPFP RTVVAVEVQD LKNGATHYWS LEKLKQRLDL MREMYDRAGE MASSAQDESE
ATMTGSDPFY DRFHWFKLVG SSPIFHGCVN ERLADRTPSP TFSTADSDIT ELADEQQDEM
EDFDDEAFVD DTGSDAGTEE GSDLFSDGHD PFYDRSPWFI LVGRAFVYLS NLLYPVPLIH
RVAIVSEKGE VRGFLRVAVQ AIAGDEEAPD YGSGIRQSGT AKISFDNECF NQSDFSSVAM
TRSGLSLEEL RIVEGQGQSS EVITPPEEIN RMNDLDLKSS TLLDGKMVME GFSEEIGNHL
KLGSAFTFRV TVLQASGILP EYADIFCQFN PPQPSRRFFP PPMPLSKPDH ERKIELIRFL
VSDYVNVHVL DTFSEHASVF ASSAIATFQD GADPLPPFLL LPIPSCQSER VPKRDGTSQL
WLTIQQAYPA RGHFCFTSQK FLIGIEDEDF RGLKIWPGNG IQRRITVTII HEKGSELHWK
DVRELVVGRI RNKAEVDEAA IDAILSLNII SAKYLKSSHN SSRTFYRFEA VWDSSLHNSL
LLNRVTPYGE KIYMTLSAYL ELDHCIQPAV ITKDVCMVFY SRDAKISPPR SLRSLFGSGY
SKSPDSNRVT GIYELSLCKM ADTGSPGMQR RRRKILDTSV AYVRGEENLA GWRPRGDSLI
LEHQWELEKL ELLHEVEKTR HFLLLRERLG DSIPKSLSDS LSPSLSSGTL STSTSISSQI
STTTFESAIT PSESSGYDSA DIESLVDREK ELATKCLQLL THTFNREFSQ VHGSISDCKL
SDISPIGRDP SVSSFSSATL TPSSTCPSLV DARSNSLDQK TPEANSRASS PCPEFEQFQI
VPTVETPYLA RAGKNEFLNL VPDIEEIRPG SVVSKKGYLH FKEPLSSNWA KHFVVVRRPY
VFIYNSDKDP VERGIINLST AQVEYSEDQQ AMVKTLNTFA VCTKHRGVLL QALNDKDMSD
WLYAFNPLLA GTIRADIALI GLAVMGQNLI LNMNDHGFVV CAFNRTVSKV DDFLANEAKG
TKVIGAHSLE EMVSKLKKPR RIILLVKAGQ AVDDFIEKLV PLLDTGDIII DGGNSEYRDT
TRRCRDLKAK GILFVGSGVS GGEEGARYGP SLMPGGNKEA WPHLKTIFQS IAAKVGTGEP
CCDWVGDEGA GHFVKMVHNG IEYGDMQLIC EAYHLMKDVL GMEHKEMAQA FEEWNKTELD
SFLIEITANI LKFQDTDGKH LLPKIRDSAG QKGTGKWTAI SALEYGVPVT LIGEAVFARC
LSSLKDERIQ ASKKLKGPQK TQFEGDKKSF LEDIRKVGPG LAAAVWVGGA VGEHPDATHG
GAALYASKII SYAQGFMLLR QAATEFGWTL NYGGIALMWR GGCIIRSVFL GKIKDAFDRN
PGLQNLLLDD FFKSAVENCQ DSWRRTVCTG VQTGIPMPCF TTALSFYDGY RHEMLPANLI
QAQRDYFGAH TYELLAKPGQ FIHTNWTGHG GSVSSSSYNA
//
