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Database: UniProt
Entry: A0A094EMQ8_9PEZI
LinkDB: A0A094EMQ8_9PEZI
Original site: A0A094EMQ8_9PEZI 
ID   A0A094EMQ8_9PEZI        Unreviewed;      1536 AA.
AC   A0A094EMQ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=V499_01066 {ECO:0000313|EMBL:KFY80026.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY80026.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY80026.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY80026.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00033655};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603437-50};
CC   -!- SIMILARITY: Belongs to the GcvP family.
CC       {ECO:0000256|ARBA:ARBA00010756}.
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:KFY80026.1}.
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DR   EMBL; JPKB01000109; KFY80026.1; -; Genomic_DNA.
DR   HOGENOM; CLU_004620_3_1_1; -.
DR   Proteomes; UP000029295; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 2.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF13673; Acetyltransf_10; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50}.
FT   DOMAIN          1..179
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REPEAT          390..422
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   MOD_RES         1285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   1536 AA;  168798 MW;  8119ED6E744DB7EF CRC64;
     MIMFPNADPS PEEEEEETKW SIEYLQESLQ NDSCYFRKVT DSSGCYAGFA IWTLDPSSTV
     TGHKTKSTQK RRESWNPASL DVRAWIEVSN LLREERQRVL NGQHNIWRLN TISVTPEHQR
     QGVGSMLMQW GCDKADSCGW NSFVMASPDG VPLYTKFDFK VVGQVQIKHG AFTTAAPLPF
     ANPNIDALRR EIRAGNLPGV QNTFSEWLED DPSNISKIGR LYLCIGDAIE CSQHEILTYL
     LSEGFPLDMF DISLATRRKE RCALEILIAH GWNINKPRTN RDPPLLSQAI KDEKLASWFL
     DHGANPNAEC DFDFTPLSAA MVSASFATIK LLFDRGGSVK HGQLLHYVAR RSGPDPIKIL
     DFILSKGAPG MNRLLHQHRP ADYLPLEYAG LSTPLGMAAR EGTLDIARYL LKSGADPTIK
     NSLGYLPIET AEYYNNHDIV TLLSEFELKL SWRDRVDAAD TSRPARGSIF KMAAIRSAMR
     TNLRQLASRP RAPLSRGSRA WAGNQCPLSV TTTTSAGLRT YYKSAPADPA NRAVSPKEER
     DVFAPLDSFA RRHIGPTPSA TEAMLKVLNP PVKSLDEFVE SVVPSSILTA KELKIDGPSK
     GVMVDNLPIN EEGYSESQLT TRLKSIASKN KILRSYIGCG YAGTRTPEVI KRNVLESPGW
     YTSYTPYQPE ISQGRLESLL NFQTMVSDLT ALPIANASLL DEPTAAAEAM TLSMNMLPAS
     KQKRANKTFF VSHLVNPQTV SVLQSRADGF GIKIETGDVL KNGSARVNEL GDDLVGVLVQ
     YPDTEGGVED FKALADIVHG HGSTLSVATD LLALTVLTPP GEFGADIAFG NAQRFGVPFG
     YGGPHAAFFS VSEKYKRKIP GRLIGVSKDR LGDRALRLAL QTREQHIRRE KATSNVCTAQ
     ALLANMSAFY AVYHGPKGLK AIAERTIACT RILEEGIKRL GFETGSRGKD DEGRALFDTI
     TVNVGNGKAQ EVLSWAVKER GINLRMFDES RVGITLDETI EEHDLQDLLS IFTQFAPKKA
     DIQLAQIGKE LNGTTAKTSK PLIRTSEYLT HPVFNSHHSE TELLRYINHL QSKDLSLTHS
     MIPLGSCTMK LNSTTEMIPV TWPEFSSIHP FAPVDQATGY KTLIDELESD LATITGFDAV
     SLQPNSGAQG EFAGLRVIRK FHEQQQGGAK RDICLIPVSA HGTNPASAAM AGMRVVTIKC
     DTKTGNLDMA DLKAKCEKHS AQLGAIMITY PSTFGVFEPE VKAACELVHQ HGGQVYMDGA
     NMNAQIGLCS PGEIGADVCH LNLHKTFCIP HGGGGPGVGP IGVKSHLAPF LPGHPLITTG
     GEHAIAPVSG APWGSASILP ISWSYVKMMG GRGLTHATKI TLLNANYLMS RLRDHYPILY
     TNDAGRCAHE FILDVRGFKE TAGIEAIDIA KRLQDYGFHA PTMSWPVANT LMIEPTESES
     QEELDRFADA LIAIRAEIKD VEEGRVAKGE NVLTMSPHTQ RDLLVGEWNR SYTREQAAYP
     AEWLKEKKFW PTVTRLDDSY GDLNLFCTCS PVDAIE
//
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