ID A0A2G2AEA4_9RHOB Unreviewed; 855 AA. AC A0A2G2AEA4; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 10-OCT-2018, entry version 6. DE RecName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|SAAS:SAAS00731728}; DE EC=1.4.4.2 {ECO:0000256|SAAS:SAAS00731728}; DE Flags: Fragment; GN ORFNames=COB65_01270 {ECO:0000313|EMBL:PHQ86354.1}; OS Thalassobium sp. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Thalassobium. OX NCBI_TaxID=2030825 {ECO:0000313|EMBL:PHQ86354.1}; RN [1] {ECO:0000313|EMBL:PHQ86354.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NORP134 {ECO:0000313|EMBL:PHQ86354.1}; RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.; RT "A dynamic microbial community with high functional redundancy RT inhabits the cold, oxic subseafloor aquifer."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Glycine + [glycine-cleavage complex H CC protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H CC protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO(2). CC {ECO:0000256|SAAS:SAAS00731757}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|PIRSR:PIRSR603437-50, CC ECO:0000256|SAAS:SAAS00652867}; CC -!- SIMILARITY: Belongs to the GcvP family. CC {ECO:0000256|SAAS:SAAS00731791}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PHQ86354.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NVST01000015; PHQ86354.1; -; Genomic_DNA. 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; 1. DR Gene3D; 3.40.640.10; -; 2. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR003437; GcvP. DR InterPro; IPR020581; GDC_P. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR PANTHER; PTHR11773; PTHR11773; 1. DR Pfam; PF02347; GDC-P; 2. DR SUPFAM; SSF53383; SSF53383; 2. DR TIGRFAMs; TIGR00461; gcvP; 1. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|SAAS:SAAS00731778, KW ECO:0000313|EMBL:PHQ86354.1}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50, KW ECO:0000256|SAAS:SAAS00652870}. FT MOD_RES 699 699 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|PIRSR:PIRSR603437-50}. FT NON_TER 855 855 {ECO:0000313|EMBL:PHQ86354.1}. SQ SEQUENCE 855 AA; 93080 MW; A04BAB2FBB114D68 CRC64; MSFTPTDYLP YDFANRRHIG PSPAEMAQML EVIGVASLDQ LIDETVPKEI RQAEPLDFGK AKSERELLHH MRKVAGKNKV YTSLIGQGYY GTVTPPAIQR NILENPAWYT AYTPYQPEIS QGRLEALINF QTMIIDLTGL DIANASLLDE ATACAEAMVM AQRVAKSKAG AFFVDHHCHP QNIAVMQTRA APLGIKVIVG DPADMDPEAV FGAVFQYPGT YGAVHDFSDP IAALHGAKAI GIICADPLAL TLLKEPGAMG ADIAVGSTQR FGVPVGYGGP HAAYFACKDA YKRNMPGRIV GVSIDSHGHQ AYRLSLQTRE QHIRREKATS NVCTAQALLA VMASFYGVFH GPEGLKAIAQ RIHRKTVRLA KGLEEAGFDI GTGAFFDTIT VKVGKDQAKI MQAAVDRQIN LRRVGDDRIG ISLDETTRPK RVEKVWEAFG IKRKDRNFDP EYRVPDELHR TSDYLTHPVF HMNRAETEMM RYMRRLADRD LALDRAMIPL GSCTMKLNAA VEMMPVSWRE FSLVHPFAPR DQTEGYQELI TDLSAKLCEI TGYDAMSMQP NSGAQGEYAG LLTIAAYHRA NGDDQRKVCL IPVNAHGTNP ASAQMCGMEV VVVKCTERGD IDTEDFRAKA AAAGDTLAAC MITYPSTHGV FEETVREVCE ITHEFGGQVY LDGANLNAMV GLSKPGEIGS DVSHLNLHKT FCIPHGGGGP GMGPIGVKAH LAKHLPGHPQ TGGEQGPVSA APYGSPSILP ISWAYILLMG GAGLTQATRV AILNANYIAK RLEGAYDVLY KGTRGHVAHE CILDTRPYAD SAHVNVDDIA KRLMDCGFHA PTMSWPVAGT LMVEPTESET KAELD //