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
//