ID A0A2B4S4K1_STYPI Unreviewed; 2005 AA.
AC A0A2B4S4K1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase {ECO:0000256|ARBA:ARBA00015587};
DE EC=4.2.3.12 {ECO:0000256|ARBA:ARBA00013100};
GN ORFNames=AWC38_SpisGene10555 {ECO:0000313|EMBL:PFX24831.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX24831.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005126}.
CC -!- SIMILARITY: Belongs to the PTPS family.
CC {ECO:0000256|ARBA:ARBA00009164}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:PFX24831.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSMT01000166; PFX24831.1; -; Genomic_DNA.
DR STRING; 50429.A0A2B4S4K1; -.
DR EnsemblMetazoa; XM_022936194.1; XP_022791929.1; LOC111331136.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00470; PTPS; 1.
DR Gene3D; 3.30.479.10; 6-pyruvoyl tetrahydropterin synthase/QueD; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022470; PTPS_Cys_AS.
DR InterPro; IPR022469; PTPS_His_AS.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR Pfam; PF00225; Kinesin; 2.
DR Pfam; PF01242; PTPS; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00987; PTPS_1; 1.
DR PROSITE; PS00988; PTPS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Tetrahydrobiopterin biosynthesis {ECO:0000256|ARBA:ARBA00023007}.
FT DOMAIN 151..442
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 282..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 458..550
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 815..856
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 912..946
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1192..1268
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1376..1410
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1455..1482
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1523..1584
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1617..1706
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 285..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1851..1872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2005 AA; 226462 MW; CA75CAB93FDC10A6 CRC64;
MNGKETNTLP VVYISRKETF CASHRLHSAK LSDDENRLIF GKCNNKNGHG HNYTVKVTVY
GPVNPLNGMV MNLTDLKAHM GSVLEPLDHK NLDLDVPYFK DVCSTAENIA VYIWNSLSTR
LPKSTLFEVK IDETGKNSAR YRGEMSAQCP GKTHTLMAPD GITAGVIERC FKRITKDDYH
DYKVTMSYLQ IYQEKIYDLL NSTNKVELSL REHPVKGVYV ENLTEFVVRS PSEVLHLLAV
GKKRLIFAET KMNRNSSRSH SVCQLTIERT LNKNKMNAEG IAKHGANGRD SRDGLVPSKT
SSDHEDSGED LDAGASEAND NEEDESLAKM VAFDDDVLIR GRIYLCDLAG SERLKKTQAE
GERLSEAQHI NLSLLELGNV IQALAEGKKT HVPFRNSTLT RLLQESLGGN CKTSLVVCVS
PTMGDVSETK STLFFGSRAM KITNTAYINV EVDYKRLSED LSKIVDRREK DLEDLKQTFE
TRIERLKHEA ERTVTNAMAE ADRVVASVKS LYENEKSSLE SDIENLNFRL DEEKTHTENL
QDQITKAKGK LQEDMFKARS TLLSDIISMQ LLYALKDLPL DNDHHFSEND LSLRDFCSQW
ATTKCKILEN ADVLLDLLKS YLSLMNSKGD KLLEDGGSLK SLVGCEESFN ADKRLLSASE
EVSLYMTNKT DDDKVVASTG CCEILPCSET NTEDFILSTE QNLGDGEESS NIRNKLISLK
KFMDDKALAF LTKAFELDVG NENRVINTRQ DIYGRIQEIL NQEDTLPDFR ENAAELSHVA
DALGLLDHCH SHVIVDKALQ GALLVLENNI VIKRCNVIQK QKDVLQDENE TLRKQIQILQ
KEAEKLNGKL NETSSSLCDV MKSKEQLEDD LSSVFQLHNM RNIERKIQKE NDGKLDMSTI
LQENVTTLLE NNTKLQETLQ VSENDKENLK SELTSVKEEL QRLKEGYVQD EKGTQTDLVG
QNEFMKPHLG DQSKTISDRN GIIHAILSSL HDDQSSLLEK AAFAAQSNNV DDVSSLRAVI
NHRLGEEWSL VVLENARMKS ELDGILGRIN EEKRNLVSEL ADWKFQAAEV NSMKEELNTK
GEDFADGFKV PMDENENGSS DKLISKIDIY NQNEVIAELR MDEQEDKGEP RREGSTAGDY
WESIVKEKLG ELSVVHRETE RHEVIELDSL ESKYSDPEKD QDNSNKIREK ELRELLKRER
QLTTNIMQLD EKCSSLEKQL GRSALENTKL KEQLRKLKIK ISDVEQEKAE ITAQKIALEE
SSRELQQNAK REIAVEKERT LTLEKQLQAK TQEFGEGKAL LKLKDARVSE VEAELLETKA
YYKKLLQENS HEYEVDQQNM MKEINSLRCL QGLPTLKKDS VQSKQEVKGG LMNGENQAEN
KKDNKLNSEL TRAKEQLVRL KAELTLSNMQ TRNLGSQLSS LREDSTKLEA ELSTVRVSPR
NSRQRRASFS FYEETVRLEM ELAEAKEKII DLQEKLLIIY KEKFALEEKI VSLEGQRNVH
LENGAKLYSA NDDHEPFCDL EKTKVLKSKI GLLEAEKEQL KRELDNTNAD KTRLESIEHC
VQQLVSLEDE HLRVKDRLKK WAQNSTDEQQ LNETRKTVNK FPENSYFNEL RVLSGENLVL
QEEVSGLRET IAQLESDLAA LKLKLSIADA AQDDSLDKKT VATLLVSVKQ ERAELQKALN
DALIEKDDLD EELSEIKVKY AKLQREFAMT SIVKDDLELE VLSLKKASLA RGLSNLTQSS
EDCKSEMSDS SVDDKLIDRS DENGVGDSMD KKIASPGGGR KRAPALNSRK TVITKNLKAE
RDSFSSGRST SSSSSKNEKK TLSQRPNSLQ SVPLPPKKSV ERRAKSSESG GEKLSSRTPR
SITDDQSTDD NPQHLAICYD LIRIDDAVSE ACARHVNTDC INSGLLRKTP EGQRLNPEGM
EHDNETCFDT DNTEHVDKKD SSDNFLDDTV EIGAHQGATE GISETDFSLS QSTEVLVKTT
WSLKNLFRWQ KSAPIPDHKI DALTQ
//
