ID D8JAM1_HALJB Unreviewed; 475 AA.
AC D8JAM1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN OrderedLocusNames=HacjB3_06780 {ECO:0000313|EMBL:ADJ14743.1};
GN ORFNames=C497_05187 {ECO:0000313|EMBL:ELY39325.1};
OS Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS 4019 / B3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halalkalicoccus.
OX NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ14743.1, ECO:0000313|Proteomes:UP000000390};
RN [1] {ECO:0000313|EMBL:ADJ14743.1, ECO:0000313|Proteomes:UP000000390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ADJ14743.1}, and DSM 18796 / CECT 7217 /
RC JCM 14584 / KCTC 4019 / B3 {ECO:0000313|Proteomes:UP000000390};
RX PubMed=20601480; DOI=10.1128/JB.00663-10;
RA Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT halophilic archaeon.";
RL J. Bacteriol. 192:4528-4529(2010).
RN [2] {ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|Proteomes:UP000011645};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY39325.1, ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ELY39325.1,
RC ECO:0000313|Proteomes:UP000011645};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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; CP002062; ADJ14743.1; -; Genomic_DNA.
DR EMBL; AOHV01000015; ELY39325.1; -; Genomic_DNA.
DR RefSeq; WP_008415013.1; NZ_AXZD01000007.1.
DR AlphaFoldDB; D8JAM1; -.
DR STRING; 795797.HacjB3_06780; -.
DR GeneID; 9419157; -.
DR KEGG; hje:HacjB3_06780; -.
DR PATRIC; fig|795797.18.peg.1354; -.
DR eggNOG; arCOG00076; Archaea.
DR HOGENOM; CLU_004620_5_0_2; -.
DR OrthoDB; 371967at2157; -.
DR Proteomes; UP000000390; Chromosome.
DR Proteomes; UP000011645; Unassembled WGS sequence.
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 ECO:0000313|EMBL:ADJ14743.1}.
FT DOMAIN 147..277
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 348..443
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51146 MW; 43C112308CBCE033 CRC64;
MTLEYTQARW NTDDEGYEPL LAEKNEETVD TDDVPLPDDL KRDSLTLPEL SEPELARHYT
RLSQMNYGVD SGPYPLGSCT MKYNPKFTED VAALSSAGVH PDRSPGSVQG TLELLARLEE
QLGRIGGMDA VTLQPPAGAA GEFVGILIAK AYHESRDDER TEVVIPDAAH GTNFASAALG
GYDVVELPSG EDGRVDLDAL EAALSEETAA LMLTNPNTLG LFEREIEEIA GMVHDVGGLL
YYDGANLNAL LGRARPGDMG FDVMHYNVHK TFATPHGGGG PGAGPVGVVE ELAEFLPSPH
VRGGDSGYEL FEPESTIGKV HGFMGNWLVL IKAYAYIARL GDGGLADASA KAVLNANYLG
SRIEYEVPYS PFHHEFVASA GEQDAADVAK RMLDYGVHPP TTKWPELVGE ALMTEPTEIE
NRRSLDQLAA AFNAVASEDR AAVETAPERT TAGRIDQTEA ARNLRLSWQS LDDSS
//
