ID V6KVS1_STRRC Unreviewed; 962 AA.
AC V6KVS1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN ORFNames=M878_05605 {ECO:0000313|EMBL:EST35536.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST35536.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST35536.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST35536.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + O2 + sarcosine = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + glycine + H2O2;
CC Xref=Rhea:RHEA:70455, ChEBI:CHEBI:15379, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57453; EC=1.5.3.24;
CC Evidence={ECO:0000256|PIRNR:PIRNR037980};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRNR:PIRNR037980};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRNR:PIRNR037980};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037980}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|PIRNR:PIRNR037980}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EST35536.1}.
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DR EMBL; AWQX01000050; EST35536.1; -; Genomic_DNA.
DR RefSeq; WP_023545123.1; NZ_CM002285.1.
DR AlphaFoldDB; V6KVS1; -.
DR STRING; 1352936.M878_05605; -.
DR PATRIC; fig|1352936.5.peg.1208; -.
DR HOGENOM; CLU_011963_0_0_11; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000017984; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR006277; Sarcosine_oxidase_asu.
DR InterPro; IPR041117; SoxA_A3.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR NCBIfam; TIGR01372; soxA; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF17806; SO_alpha_A3; 1.
DR PIRSF; PIRSF037980; SoxA; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037980};
KW NAD {ECO:0000256|PIRNR:PIRNR037980};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037980};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR037980};
KW Reference proteome {ECO:0000313|Proteomes:UP000017984}.
FT DOMAIN 123..388
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 476..559
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 574..841
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 865..954
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 962 AA; 102437 MW; 31D7684AD5AA920D CRC64;
MTDQHFRRRQ GGRIDRGTVL RFTVDGRELT GHPGDTVASA LLANGLVEVA PSLYRHRPRG
IVSAGVEEPN ALVQLEGPCS EGMLPATTVE LYDGLCATTL SGMGRLDPSP DPAVYDKKYV
HTDVLVVGAG PAGLAAAAAA VESGARVILV DDQPEPGGSL LSGRTERVGS RTALQWVADV
RSALDAAPEA VVLQRTTAFG SYDDNYVLAL QRRTDHLGAD APEPSAGVSR QRLWHIRARQ
VVLATGAHER PLVFAGNDRP GVMLAGAVRS YLNRYAVAPG TRAVVSTTND SAYDTVADLH
AAGIDIAAVV DARPELSNRA AAAAGATGVR VLTGSAVVDT AGGSRITGVT VRALDDSGRL
TGDPESFACD LLAVSGGWSP VVHLHSQRQG RLRWDEELVA FVPDGTVRDQ QVVGAARGTY
DLDSALAEGA RAGARAATDA GFPVPVPPPG DARSGSGSVR ALWLVPAPDG DPGSWDTHFV
DLQRDVTVAG VWRSTGAGMR GVEHVKRYTS LGTANDQGKT SGVNAIGVIA EALGGSLGEI
GTTAYRAPYT PVAFAALAGR ERGDLFDPER TTSLHSWHVA QGAEFEDVGQ WKRPWYYPRP
GEDMDTAVAR ECRAAREGVA FMDASTLGKI EIWGADAGEF LNRIYTNAFK KLKPGMARYG
VMCKPDGMIF DDGVTLRLDD NRYFMSTTTG GAAGVLDWLE EWLQTEWPEL DVHCTSVTEQ
WATIAVVGPR SREVVAQIAP QVDLSNDEFP FMAFRETTLA SGVPARICRI SFSGELAYEI
NVCAWYGLAV WEEVYAIGRP YGITPYGTET MHVLRAEKGY IIVGQDTDGT VTPHDAGMSW
VVSKQKDFIG KRSFSRTDTS RTGRKQLVGL LPADRTTRLP EGTQLVAPGV PITPESGPVP
MLGHVTSSYH SPALGRPFAL ALVADGRART GETLLAPVGD ALVPVEVTDF VLYDPEGTKR
DG
//
