ID A0A0G4MTF4_9PEZI Unreviewed; 2906 AA.
AC A0A0G4MTF4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=threonine synthase {ECO:0000256|ARBA:ARBA00013028};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=BN1708_001505 {ECO:0000313|EMBL:CRK37484.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK37484.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK37484.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK37484.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000051};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; CVQH01024749; CRK37484.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4MTF4; -.
DR OrthoDB; 275600at2759; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01560; Thr-synth_2; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR019451; Rtp1_C1.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF10363; RTP1_C1; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SMART; SM00384; AT_hook; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2779..2806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 739..840
FT /note="RNA polymerase II assembly factor Rtp1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10363"
FT DOMAIN 1779..1856
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 1865..2097
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1044..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2874..2906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1549..1563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1666..1688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1754..1778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1888
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 2906 AA; 317571 MW; 606200FD5FCD62C3 CRC64;
MPSNTVDFKL KNTNISFNLP GHNNKMSDKY PCKYHNNPNG ACFPGIEWVG GADAACDKCL
AAGLPRGLNQ CRKWEPMSTS LCERSRDNGA IYQEIHAILE PHRQHRQHSC PARNTDKKSL
RVVLAISYVA KRFTDLLFFT WQLRTRLLAL KFLRRSSSKK RHPTNKFVGS CIQVYSSDCH
DRDMMASTGK ESRQTLADTL LDVGKRAFDP TTEPTSRDLA LKEFNSLVEG NVSWNLLPAL
SALIKPNVAP SWLQPQLMKI LTHIPLRRDG VRGTLEFVFS VHPSSQMKAS DETTLHKTGA
NITQEALAVA TRIITSPPAT TAPTQWFAGI APQIHQLLDG NEGPELSRVA AQVVMIGILS
KKQFGAPGTP GWDVFIEPLL FTINPSRPPA TFLETDSSGE QDDVLDLTRS RVLVPFDRIR
LALQRLSTLL NTTPFPAQAR RVIGPIIRQL WAIASWQNPG PQLQETCCTP ALSLLIMFFK
IGSSSAQLLK IVENLDYKGE LEPEKKMWAY ATSAPDGVEI ISMEELRDPR LHQIDWSGVR
HKSSAFVSLM ATSCTPDEVS SFAMDLLSRW MADLVASAPA QPKIKLEEAE PDEKGLQLKK
LWEVSILQNM LEEVPEKLIS RIEQVLELVC QILNPETLQS QSDDIIAVAL SLLNLVITSP
TFKRSNLKPR GLEVLETSLE KLGSGNHPTV SPTARNLGLL LQYRDAAGGE DEKDGFVPNA
KQVEDRATYK LAISYITQAD NPPPVRSEGL NLISSLILAN STALDVQAVL VLLSSLMQDA
EDYINLRVIK VFTQMANKHP KATSREILDH YLDPKERSTT DTRLRFGEAL LQVIERLGET
FAGDVARHVT ETLLSIAGRR GYRPQTEARQ AREARRREIK KKQAEDAWDG EVPDLGDELT
EEEQATSDVL TQIVEGWESK RGSEDVRMRS SALSILAGAM ETNVSGVGPD LVSASVDLCV
NVLTLEPELE RGILRRAAVL LILSFVKALD VARQTGRRIG FGLTDSSRND ILRVLKYIAI
SDNDGLPCLR VTTMATHNII ADSDEEDDFT PGQSPMKPQT PVIAPASRSP TTGNGTDSTD
PRFFQAIYSE QQQAVERAAP TRADHSFDAA DNTSSSISLN AHLQKKTGIE NTSSLTSVSD
PVPRRPRAAH LVSPSGVTQL SPPARNVAST MKDVWDIPSS PEATSLPMPK RSLISHATGH
STTFAKYANA GRAFSPTSEA APSSGLSDPP VEATTERDDV ATPPRHADQQ WPQHAGLASP
TQQNSPTRIS AARHCPVSGQ KPTAPLASDS LLSEQTASMP GLAAICIEPT TLSTSQRALY
QSLHPSPEEE TVQDFDGAAH FKQAMSGMRS SGATTIAYAT PSQWQKSSHP VVVEPKEASS
PVTSRKKRAR GLVDAEPASS PDLLAVEERP GKRGKTAERK TDKATARRSA TRQVKDSDDD
DEDEGAGEDD DDDGFTAEAY QPRPSWRRAI GARLRGVEGN AEEEEQMAAI AAATHVAETQ
KPPKALLAAE SDSPPPRKKR GRPKKAEMPT TPQVNEPLSD GQPHIVEDAQ GPSDTTDQAV
DALETDQHAQ APPAEVAKPG KRKRGRPRKS DQAATPKAAP VEVPVEMPVV CVDDVTSGTT
MDGAATDGPA GGLPEEDVPT VTPHARVDKR ALGDASGNPI QSADDVVKMD KVETREHERD
ERDATPAKPK AAESTATSTK REPQLPVTPQ AGKPLYRVGL SKRSRIAPLL KSLRKTAGME
RVAKEYPDRL KMASNGTTPH NGVGNVGSGG DSDHTPSQRY LSTRGEDTDF SFEEVVLKGL
ASDGGLYIPS EIPQADNWQS WKDKSFTELA FEILSLYISP AEIPSEDLKG IIERSYSTFR
APETTPLRHL NDNLYLLELF HGPTFAFKDV ALQFLGNLFE YFLVRKNEGK TGRDRHHLTV
VGATSGDTGS AAIYGLRGKK DVSVFILHPK GRVSPIQEAQ MTTVLDDNVH NLAVTGTFDD
CQDIVKALFA DPEINKTHNL GAVNSINWAR ILAQVVYYFH AYFALIKSSE TLKLGDKVRF
VVPTGNFGDI LAGYFAFRMG LPVAKLVVAT NENDILHRFW TTGRYEKHEA HGAEATGGLA
QDGAKAHEDG AKETLSPAMD ILVSSNFERL LWFLAYEFAS SVGMGDEWNK KQAGQEVTTW
LSELKTKGGF GPVYKDVLAS ARRDFESERV SDEQTTETIR NLYNSSAAYV LDPHTAVGVA
ASLRSIERSG PEVPHISLST AHPAKFAGAV ELALKDEAGF DFAGKVLPQE FVGLESKEKR
VSEVAADWKQ HSISMRCTQG RRLGIEPVQP EQDPEQTTCA NHGVTPFMLV QPDVLSWVVW
GSVAVIMNGE RTPLRGGLAS TITPQGAQQM YGQGVAFRHR YIDGTNAQDN IFRAPIRGIE
RDTLDNSQLT ILTNTDVHTI AGATAFLQGL YPPVDDEFLD EAGGVSLSYD AATDNYTQYP
LNGYQYPAIS TLSTLEETSI PLHGHKGCFN WLNAMDKLPE DENIRKEADA TLESYQKIFS
SLPLDGAFAD DFPSFWNAYD VFDYVRYQSN HNSTIHRQLE EPVLSEPTLE FLERNAFKQQ
LALNTDSSLS GASTRDPVRS IAGQALAQGI LDALAAVVSS RGETDKLTLM FTSFHPFIAF
WSLTQLLTTT TDPSSPYASF PAPGFSMSFE LIGDQPGQPG QFPSNDDLRV RFVIRNANST
TTFRADNIFG TPVSEYIMPL DLFATQMRNI AIDVGEWCIH CSSPQLFCVA RSALAADGSD
GDSSGRNKDG SRSLSSTPVV VAMLGAAVML ILVALVAAVA AFFFGVRFHR PGKGSFRGAE
KRAEDADVVV SRGGARHERV GSWELRDGRD VTADEAHFRD SKFSGAGLVF DKETGRTSER
ETADDDGVSV LSTDITAQPV RPRESV
//
