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
//