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Database: UniProt
Entry: W0JN38_9EURY
LinkDB: W0JN38_9EURY
Original site: W0JN38_9EURY 
ID   W0JN38_9EURY            Unreviewed;       490 AA.
AC   W0JN38;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=HALLA_15590 {ECO:0000313|EMBL:AHG00009.1};
OS   Halostagnicola larsenii XH-48.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG00009.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHG00009.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHG00009.1,
RC   ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JAN-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:ARBA00043839};
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DR   EMBL; CP007055; AHG00009.1; -; Genomic_DNA.
DR   RefSeq; WP_049953247.1; NZ_CP007055.1.
DR   AlphaFoldDB; W0JN38; -.
DR   STRING; 797299.HALLA_15590; -.
DR   GeneID; 25145842; -.
DR   KEGG; hlr:HALLA_15590; -.
DR   PATRIC; fig|797299.3.peg.2123; -.
DR   eggNOG; arCOG00076; Archaea.
DR   HOGENOM; CLU_004620_5_0_2; -.
DR   OrthoDB; 371967at2157; -.
DR   Proteomes; UP000019024; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   Gene3D; 6.20.440.10; -; 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); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT   DOMAIN          165..293
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          365..462
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   490 AA;  53158 MW;  1CF817E03D4EB12A CRC64;
     MSDDNAREAP GTVDPSGRSR YDQARYVRNG QYEPLLVEKD RTRVEIDESP LPEDLTRDDL
     ELPDPSEPEL VRHYTRLSQM VYGIDSGPYP LGSCTMKYNP KFTEDVASLP SALVHPDRSE
     ESIQGTLEVL ARLQEYLEVI GGMDAVTLQP PAGAAGEFVG IRVAAAYHEH TDEGQRDEVI
     IPESAHGTNF ATAALGGYDV VSLPSDEGGR VDLEALEAAL SENTAALMLT NPNTLGLFER
     DIETIAEMVH DAGGLLYYDG ANLNALLGRA RPGDMGFDVM HYNVHKTFAT PHGGGGPGAG
     PVGVVSELAP FLPEPRVRNA DGGYELFAPE HSIGHVHGYQ GNWLVLVKAF AYIARVGDDG
     LTDSSAKAVL NANYLASQIE YDVPYGPFHH EFVASAGEQD AADVAKRMLD YGVHPPTTKW
     PEIVPEALMT EPTEIESKET LDQLAAAFNA VAEEGAEILE SAPERTTARR IDQTSAARNP
     RLSWHALEEE
//
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