ID A0A1P8W8S0_9PLAN Unreviewed; 431 AA. AC A0A1P8W8S0; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 07-NOV-2018, entry version 8. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|HAMAP-Rule:MF_00375}; DE Short=GSA {ECO:0000256|HAMAP-Rule:MF_00375}; DE EC=5.4.3.8 {ECO:0000256|HAMAP-Rule:MF_00375}; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|HAMAP-Rule:MF_00375}; DE Short=GSA-AT {ECO:0000256|HAMAP-Rule:MF_00375}; GN Name=hemL {ECO:0000256|HAMAP-Rule:MF_00375, GN ECO:0000313|EMBL:APZ90456.1}; GN ORFNames=Fuma_00030 {ECO:0000313|EMBL:APZ90456.1}; OS Fuerstia marisgermanicae. OC Bacteria; Planctomycetes; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Fuerstia. OX NCBI_TaxID=1891926 {ECO:0000313|EMBL:APZ90456.1, ECO:0000313|Proteomes:UP000187735}; RN [1] {ECO:0000313|EMBL:APZ90456.1, ECO:0000313|Proteomes:UP000187735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NH11 {ECO:0000313|EMBL:APZ90456.1, RC ECO:0000313|Proteomes:UP000187735}; RX PubMed=28066393; DOI=10.3389/fmicb.2016.02079; RA Kohn T., Heuer A., Jogler M., Vollmers J., Boedeker C., Bunk B., RA Rast P., Borchert D., Glockner I., Freese H.M., Klenk H.P., RA Overmann J., Kaster A.K., Rohde M., Wiegand S., Jogler C.; RT "Fuerstia marisgermanicae gen. nov., sp. nov., an Unusual Member of RT the Phylum Planctomycetes from the German Wadden Sea."; RL Front. Microbiol. 7:2079-2079(2016). CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5- CC aminolevulinate. {ECO:0000256|HAMAP-Rule:MF_00375, CC ECO:0000256|SAAS:SAAS01090807}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00375, CC ECO:0000256|SAAS:SAAS01090802}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 2/2. {ECO:0000256|SAAS:SAAS01090801}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00375}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375, CC ECO:0000256|SAAS:SAAS01090808}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. {ECO:0000256|HAMAP- CC Rule:MF_00375, ECO:0000256|SAAS:SAAS01090804}. 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; CP017641; APZ90456.1; -; Genomic_DNA. DR RefSeq; WP_077022353.1; NZ_CP017641.1. DR KEGG; fmr:Fuma_00030; -. DR KO; K01845; -. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000187735; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00375; HemL_aminotrans_3; 1. DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00713; hemL; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000187735}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|SAAS:SAAS01090797}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|SAAS:SAAS01090803, ECO:0000313|EMBL:APZ90456.1}; KW Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|SAAS:SAAS01090799}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00375, KW ECO:0000256|RuleBase:RU003560, ECO:0000256|SAAS:SAAS01090798}; KW Reference proteome {ECO:0000313|Proteomes:UP000187735}. FT MOD_RES 271 271 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00375}. SQ SEQUENCE 431 AA; 45074 MW; D3A179497B0F4CF0 CRC64; MNDTANRPNS ETEFARACKS IPGGVNSPAR AFGAVGGTPP YIQRGDGPYL FDIDGNQYID FIGSWGPHIL GHRHPAVIRA IQLALETGTS FGAPTVAESE LAELVVKLVP SVEKVRMVNS GTEATMSAIR LARGFTGRDV IIKFAGCYHG HVDSLLVQAG SGALTLGTPS SPGVPSGCTA DTLVLPYNDV AALGTAFEGK GAELAAVILE PVCGNMGCVV PTEEFLQALR QTCTNNGTVL IFDEVMSGFR VALNCAQSRL GVTPDLTTLG KILGGGMPVG AYGGRADIMD AVSPVGSVYQ AGTLSGNPVA MASGLATLQQ LVKDDPYNKL ESLAAQLEDG LLAAAKNANV PVQINRVGSM LTMFFNEQPV TDFATATASD TDRFAKWFHG MLDRGVYLPC SQYEALFVSA THTPELIDET LEAASATLAT L //