ID H9UGE1_SPIAZ Unreviewed; 1340 AA.
AC H9UGE1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
DE EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616};
GN OrderedLocusNames=Spiaf_0481 {ECO:0000313|EMBL:AFG36584.1};
OS Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG36584.1, ECO:0000313|Proteomes:UP000007383};
RN [1] {ECO:0000313|Proteomes:UP000007383}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC {ECO:0000313|Proteomes:UP000007383};
RX PubMed=23991249; DOI=10.4056/sigs.3607108;
RA Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT Rift.";
RL Stand. Genomic Sci. 8:165-176(2013).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein. {ECO:0000256|ARBA:ARBA00003788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000256|ARBA:ARBA00043710};
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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DR EMBL; CP003282; AFG36584.1; -; Genomic_DNA.
DR STRING; 889378.Spiaf_0481; -.
DR KEGG; sfc:Spiaf_0481; -.
DR PATRIC; fig|889378.3.peg.490; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_12; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000007383; Chromosome.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR049315; GDC-P_N.
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 InterPro; IPR027266; TrmE/GcvT_dom1.
DR NCBIfam; TIGR00461; gcvP; 1.
DR NCBIfam; TIGR00528; gcvT; 1.
DR PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000007383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..260
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 283..360
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT DOMAIN 380..812
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 823..1109
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 1166..1287
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 1088
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 1340 AA; 145744 MW; F969675E1B5F56D1 CRC64;
MDLRTTPLDA EHRALGAKMA GFAGWQMPLH YPAGAIEEHR LVRHSAGLFD ISHMGRIEVH
GHQAVDALSH LLTADIRRLA PFEACYALLC GPDGGILDDV FVYRLADRCL VVVNAANCSR
DLAHMREHSA GFAAAFRDIT SSTAMLALQG PSALAAIEPL LGRSVDWPRL YLHEGVLHDA
PVLLCRTGYT GEDGLELICP ADTAVALWRD LLEAADTAGI QAGPAGLAAR DSLRFEPGFP
LYGNELTPHI TPVEARLMWA CRMDHEFIGR EAIIERKASP AIRLVSFVME QPGVPRHGCE
VYSPDGQRIG WVTSGLRAPS LNAFAGNAYV ETAWAGRDQE LLIEIRGSRK LARTARRPLY
RPSYRASRLP AQPEYGELVQ RHIGPTAAQR DAMLKAIGCP DMPTLIQQTI PDDILHRTAL
RLPAAAGEQE LQAELAAIAG RNIVHHPLIG QGYYGTILPA VIRRNILENP AWYTQYTPYQ
AEISQGRLEA LLNFQTMIID LTGLEAANAS LLDEATAAAE AMLLCRRAMP RSSTADHFFL
DAECHPQTLE VVSGRAEAQG IHLVVGNTEQ LMELLQHPDR VFGGLFQYPG STGAARIPRE
EIQALHDAGA LAAVAADPLA LTLLPEPAAF GADIAIGSTQ RFGQPLGFGG PHAAYIAARD
GLLRQIPGRL VGVSRDRLGN SAIRLALQTR EQHIRRDRAT SNICTAQVLP AILASMYAVY
HGADGLREIA TRIRRYTWAV AELLRRRGYQ LSSLPGFDTI TITGLQPEEC RGLMMRAEHL
GYLLRRSGPR QLSLSLDETV AEHDIVRLLQ AFPVCTPDGR VSEHLFSITC AELEQLLDAC
PELPAELQRR SSFLQAEAFI RGRSETEIQR YMARLQQRDL SLTHSMIPLG SCTMKLNPAI
AMEAITLPGF ANLHPFAPAG HARGYRDLIA ALSDYLARIT GLPGVTMQPN SGAQGEYAGL
MIIRAYHRSR GDQERTICLV PDSAHGTNPA SAVMAGYRVV TLPSAANGSI DLAALDQQLQ
QHADSVGAIM ITYPSTHGVF DENIRAVTRK VHDAGGQVYL DGANLNAMVG LSSPAAVGAD
VCHLNLHKTF AIPHGGGGPG MGPVCTAAHL IPFLPPQGYY DTAAAIPDGD PPPAPPVSAA
PFGSPGILPI TYAYIRMMGP AGLRLASETA VLNANYIAAR LQEHYPISYR NARGRVAHEC
ILDLRQLQKH SGITVEDVAK RLIDYGFHAP TMSWPEPGTL MIEPTESESL PELDRFCAAM
IAIRQEIQAV TDGAVDRDNN LLRNAPHTLA ELTAADWPHP YSREQAAFPL DWVREHKFWP
AVARVDNVFG DRHPVCACPM
//